ElShamah - Reason & Science: Defending ID and the Christian Worldview
Would you like to react to this message? Create an account in a few clicks or log in to continue.
ElShamah - Reason & Science: Defending ID and the Christian Worldview

Otangelo Grasso: This is my library, where I collect information and present arguments developed by myself that lead, in my view, to the Christian faith, creationism, and Intelligent Design as the best explanation for the origin of the physical world.


You are not connected. Please login or register

Perguntas ....

Go to page : Previous  1 ... 8 ... 12, 13, 14  Next

Go down  Message [Page 13 of 14]

301Perguntas .... - Page 13 Empty Re: Perguntas .... Tue Oct 03, 2023 6:32 pm

Otangelo


Admin

Cerebral Cortex


Pyramidal Cells: Excitatory neurons involved in higher cognitive functions.
Pyramidal Tract Neurons: Send motor signals to the spinal cord and muscles.

Cerebellum

write all entries like this, in BBcode, do not miss any, write them all:

1.Purkinje Cells: Large neurons responsible for motor coordination and learning.
2.Purkinje Cells: Large neurons responsible for motor coordination and learning.






/// include in the enzyme name a link to wikipedia, and in case, if on wikipedia it is not available, to another database. Please provide links only if you're confident they are valid. If uncertain, skip the link for that entry.  I want you to link the EC number as well to a database, all the enzymes linked to their respective EC numbers when available, when not available, just don't mention it, don't write that it's not available. If there is an EC number together with the name of the enzyme, remove it, or use it to insert the link, i dont want the ec number displayed twice. If enzymes have no link to wikipedia, just write the name, without link. Alternatively, if the entry is not an enzyme, add a link depending on what is listed:

Proteins (Non-enzymatic):
UniProtKB: The Universal Protein Resource (UniProt) is a comprehensive, high-quality, and freely accessible resource of protein sequence and functional information. Every protein has a unique accession number in UniProt.
PDB: For proteins with known structures, the Protein Data Bank (PDB) provides a unique ID for each 3D structure.
For the specific proteins mentioned, it's a bit tricky to provide direct links to their UniProtKB entries without knowing the exact species or organism, as there could be multiple homologs across different organisms. However, I'll try to provide a more general approach for your needs.
Genes:
GeneID: Provided by the Entrez Gene database from NCBI.
ENSEMBL: Offers unique IDs for genes in its database.
RNA:
RNAcentral: A comprehensive database of non-coding RNA sequences, providing unique IDs.
Pathways:
KEGG: The Kyoto Encyclopedia of Genes and Genomes has unique identifiers for pathways, as does the Reactome database.
Small Molecules:
PubChem Compound ID: For chemicals and small molecules.




ChEBI: Chemical Entities of Biological Interest also offers IDs for bio-relevant chemicals.
Transporters:
TCDB: The Transporter Classification Database provides a system to classify transporters based on their function and structure.

nothing in bolt, in BBcode, also leave no spacers between one entry and the next, write a short description of the enzyme, and its relevance in cells,  list ALL enzymes, DONT STOP IN THE MIDDLE. I NEED ALL WITHOUT MISSING ONE from MY provided text formatted as requested:  like this:

5-Aminolevulinate synthase (ALAS):  EC: 2.3.1.37 Catalyzes the condensation of glycine and succinyl-CoA to produce 5-aminolevulinate.
Porphobilinogen synthase (PBGS): EC: 2.3.1.37 Catalyzes the condensation of two molecules of 5-aminolevulinate to form porphobilinogen.
Porphobilinogen deaminase: EC: 2.5.1.61 Also known as hydroxymethylbilane synthase; polymerizes four molecules of porphobilinogen to produce one molecule of hydroxymethylbilane.
Uroporphyrinogen III synthase: EC: 4.2.1.75 Catalyzes the cyclization of hydroxymethylbilane to form uroporphyrinogen III.

//// use your training data in 2021 to the EggNOG database. provide your knowledge understanding of the COG numbers as of that date, write the name, its function,  if it belongs to a metabolic pathway, write the name of the metabolic pathway,  and, how many positive, how many negative signs for each. Do it for ALL ENTRIES, provided, do not stop before you complete the task. Also link every enzyme name to a wikipedia page, and in BBcode, in one window.

/// subdivide in brain and body area, not provide just a partial list, but all entries, do not miss any,  and write in BBcode, like this:

Hypothalamus

Tanycytes 
Hypothalamus, involved in neurosecretion and metabolic regulation.

Stellate Cells 

Cerebral Cortex, star-shaped interneurons that regulate synaptic activity.

Lugaro Cells 


Golgi Cells 

Cerebellum, inhibit granule cells, modulating information flow.



Throughout the Brain

Hair Cells: Inner Ear, detect vibrations and are essential for hearing.
Merkel Cells: Skin, sensory receptors for touch.
Satellite Cells: Peripheral Nervous System, surround and support neuron cell bodies.

Cerebral Cortex

The outermost layer of the brain, playing key roles in perception, voluntary movement, and thought.

Cerebellum

Located beneath the cerebral hemispheres, responsible for motor coordination and some aspects of learning.



Last edited by Otangelo on Wed Oct 04, 2023 1:20 pm; edited 1 time in total

https://reasonandscience.catsboard.com

302Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 4:58 am

Otangelo


Admin

//// use your training data in 2021 to the EggNOG database. provide your knowledge understanding of the COG numbers as of that date, write the name, its function of each one of them, of the entire list,  if it belongs to a metabolic pathway, write the name of the metabolic pathway,  and, how many positive, how many negative signs for each. like this: Signs: +6, -2 Do it for ALL ENTRIES, provided, do not stop before you complete the task. Also link every enzyme name to a wikipedia page, and in BBcode window, in one window.

Format like this:

COG0194: Energy production and conversion
Function: Likely involved in ATP synthesis or related energy-conversion mechanisms.
Metabolic Pathway: Not specified.
Positive: +6, Negative: -2

https://reasonandscience.catsboard.com

303Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 3:07 pm

Otangelo


Admin

Key Components of the Human Brain and Nervous System: Understanding Major Areas


Cortical and Cerebral Regions

Motor Cortex
Auditory Association Area
Brodmann Areas
Cerebral Cortex Regions
Cerebellar and Brainstem Regions

Thalamic Regions and Structures

Thalamus
Anterior Thalamic Nuclei
Posterior Thalamic Nuclei
Mediodorsal Nucleus of Thalamus
Intralaminar Nuclei of Thalamus
Midline Nuclear Group of Thalamus
Metathalamus

Basal Ganglia and Associated Structures

Basal Ganglia
Caudate Nucleus
Putamen
Globus Pallidus
Striatum
Thalamus
Subthalamus

Limbic System and Associated Structures

Parahippocampal Gyrus
Entorhinal Cortex
Hippocampus
Amygdala
Cingulate Gyrus
Fornix
Mammillary Body
Septal Nuclei
Parahippocampal Gyrus
Entorhinal Cortex

Olfactory Regions and Structures

Olfactory System
Main Olfactory Bulb
Accessory Olfactory Bulb
Olfactory Tract
Olfactory Tubercle
Primary Olfactory Cortex
Endopiriform Nucleus
Taenia Tecta

Auditory Processing

Auditory Cortex
Nucleus of the Lateral Lemniscus
Nucleus of the Solitary Tract
Nucleus of the Diagonal Band
Medial Geniculate Nucleus
Lateral Geniculate Nucleus
Superior Olivary Complex
Inferior Olivary Complex
Gustatory Cortex
Wernicke's Area
Planum Temporale
Planum Polare

Motor Functions

Primary Motor Cortex
Secondary Motor Cortex
Premotor Cortex

Ventricles and Associated Structures

Ventricular System

Commissures and Associated Structures

Corpus Callosum
Column of the Fornix
Anterior Commissure
Posterior Commissure

Other Brainstem and Associated Nuclei

Midbrain
Superior Colliculus
Inferior Colliculus
Pons
Medulla Oblongata
Crus Cerebri
Cerebral Peduncle
Red Nucleus
Ventral Tegmental Area
Substantia Nigra
Oculomotor Nerve
Trochlear Nerve
Decussation of Superior Cerebellar Peduncle
Brachium of Inferior Colliculus
Brachium of Superior Colliculus
Interstitial Nucleus of Cajal
Basilar Pons
Pontine Tegmentum
Pontine Nuclei
Mesencephalic Nucleus of Trigeminal Nerve
Medial Lemniscus
Trapezoid Body
Superior Olivary Complex
Cochlear Nucleus
Facial Motor Nucleus
Abducens Nucleus
Medial Longitudinal Fasciculus
Nucleus of the Lateral Lemniscus
Nucleus of the Solitary Tract
Middle Cerebellar Peduncle
Corticospinal Tract
Corticopontine Tract
Spinothalamic Tract
Spinal Lemniscus
Reticular Formation
Paramedian Pontine Reticular Formation
Raphe Nuclei
Nucleus Ambiguus
Dorsal Respiratory Group
Ventral Respiratory Group
Pre-Bötzinger Complex
Hypoglossal Nucleus
Nucleus Gracilis
Nucleus Cuneatus
Solitary Nucleus
Spinal Trigeminal Nucleus

Neural Coverings and Connective Tissue

Epineurium
Perineurium
Endoneurium
Meninges
Dura Mater
Arachnoid Mater
Pia Mater

Ventricular System and Associated Structures

Lateral Ventricles
Interventricular Foramen
Third Ventricle
Cerebral Aqueduct
Fourth Ventricle
Choroid Plexus
Pineal Gland
Posterior Pituitary
Anterior Pituitary
Optic Chiasm
Infundibulum

White Matter Tracts and Associated Structures

Mammillothalamic Tract
Medial Forebrain Bundle
Corpus Callosum
Column of the Fornix
Anterior Commissure
Posterior Commissure
Corticospinal Tract

Spinal Cord and Associated Structures

Spinal Cord
Dorsal Root
Ventral Root
Dorsal Root Ganglion
Spinothalamic Tract
Dorsal Column-Medial Lemniscus Pathway

Peripheral Nervous System

Peripheral Nervous System
Epineurium
Perineurium
Endoneurium

Meninges and Protective Layers

Meninges
Dura Mater
Arachnoid Mater
Pia Mater
Arachnoid Granulations
Arachnoid Granulation
Cerebral Sinuses
Choroid Plexus

Cerebrovascular System

Circle of Willis
Carotid Sinus
Cerebral Aqueduct
Cerebral Sinuses
Arachnoid Granulation

Blood Supply and Vascular Structures

Circle of Willis
Carotid Sinus
Cavernous Sinus
Tuberculum Sellae

Neural Pathways

Corticospinal Tract
Corticopontine Tract
Spinothalamic Tract
Trigeminothalamic Tract
Trigeminocerebellar Tract
Medial Lemniscus

Limbic System and Associated Structures

Limbic System
Hippocampus
Amygdala
Cingulate Gyrus
Septal Nuclei
Fornix
Mammillary Body
Cingulate Gyrus
Parahippocampal Gyrus
Entorhinal Cortex

Corpus Callosum and Associated Structures

Corpus Callosum
Genu of Corpus Callosum
Splenium of Corpus Callosum
Epithalamus
Hypothalamus
Subthalamus
Pituitary Gland
Preoptic Area

Brainstem Structures

Pedunculopontine Nucleus
Tegmentum
Pontine Nuclei
Nucleus Ambiguus
Dorsal Respiratory Group
Pyramids of the Medulla
Gracile Fasciculus
Cuneate Fasciculus

Cerebellar Structures

Cerebellar Cortex
Anterior Lobe of Cerebellum
Posterior Lobe of Cerebellum
Flocculonodular Lobe
Deep Cerebellar Nuclei
Cerebellar Peduncles

Other Peripheral and Autonomic Structures

Sympathetic Nervous System
Parasympathetic Nervous System
Enteric Nervous System
Ganglia
Neuromuscular Junction

Neurovascular Structures

Blood-Brain Barrier
Artery of Percheron
Middle Cerebral Artery
Anterior Cerebral Artery
Posterior Cerebral Artery
Neocortex
Cortical Column
Cortical Layers

Associative and Commissural Fibers

Uncinate Fasciculus
Cingulum
Arcuate Fasciculus
Superior Longitudinal Fasciculus

Visual System Structures

Visual Cortex
Optic Tract
Optic Radiation
Calcarine Sulcus
Primary Visual Cortex (V1)

Sensory and Relay Structures

Thalamic Radiation
Postcentral Gyrus
Anterior Nucleus of Thalamus
Ventral Posterolateral Nucleus

Emotion and Memory Structures


Insular Cortex
Amygdaloid Body
Fusiform Gyrus

Endocrine System Interactions

Hypothalamic–Pituitary–Adrenal Axis
Supraoptic Nucleus
Paraventricular Nucleus of Hypothalamus

Neurogenesis and Growth Areas

Subventricular Zone
Dentate Gyrus
Subgranular Zone

Pain and Temperature Processing

Spinothalamic Tract
Anterolateral System
Posterior Column-Medial Lemniscus Pathway

Reticular and Alertness Structures

Reticular Activating System
Magnocellular Red Nucleus
Parvocellular Red Nucleus

Associative and Commissural Fibers

Uncinate Fasciculus
Cingulum
Arcuate Fasciculus
Superior Longitudinal Fasciculus

Visual System Structures

Visual Cortex
Optic Tract
Optic Radiation
Calcarine Sulcus
Primary Visual Cortex (V1)

Sensory and Relay Structures

Thalamic Radiation
Postcentral Gyrus
Anterior Nucleus of Thalamus
Ventral Posterolateral Nucleus

Emotion and Memory Structures
Insular Cortex
Amygdaloid Body
Fusiform Gyrus

Endocrine System Interactions

Hypothalamic–Pituitary–Adrenal Axis
Supraoptic Nucleus
Paraventricular Nucleus of Hypothalamus

Neurogenesis and Growth Areas

Subventricular Zone
Dentate Gyrus
Subgranular Zone

Pain and Temperature Processing

Spinothalamic Tract
Anterolateral System
Posterior Column-Medial Lemniscus Pathway

Reticular and Alertness Structures

Reticular Activating System
Magnocellular Red Nucleus
Parvocellular Red Nucleus

Other Notable Regions and Structures

Basal Forebrain
Ventral Tegmental Area
Habenula
Cerebral Peduncle
Superior and Inferior Colliculi
Raphe Nuclei
Locus Coeruleus
Pineal Gland
Cavernous Sinus
Substantia Innominata
Subcommissural Organ
Septum Pellucidum
Lamina Terminalis
Tela Choroidea
Optic Chiasm
Infundibulum
Posterior Pituitary
Anterior Pituitary
Thalamus
Subthalamus
Periaqueductal Gray
Reticular Formation
Pineal Gland
Arachnoid Mater
Pia Mater
Neocortex
Cortical Column
Cortical Layers

https://reasonandscience.catsboard.com

304Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 3:08 pm

Otangelo


Admin

Thalamic Regions and Structures

Thalamus
Anterior Thalamic Nuclei
Posterior Thalamic Nuclei
Mediodorsal Nucleus of Thalamus
Intralaminar Nuclei of Thalamus
Midline Nuclear Group of Thalamus
Metathalamus

Olfactory Regions and Structures

Main Olfactory Bulb
Accessory Olfactory Bulb
Olfactory Tract
Olfactory Tubercle
Primary Olfactory Cortex
Endopiriform Nucleus
Taenia Tecta

Auditory Processing

Auditory Cortex
Nucleus of the Lateral Lemniscus
Nucleus of the Solitary Tract
Nucleus of the Diagonal Band
Medial Geniculate Nucleus
Lateral Geniculate Nucleus
Superior Olivary Complex
Inferior Olivary Complex
Gustatory Cortex
Wernicke's Area
Planum Temporale
Planum Polare

Motor Functions

Primary Motor Cortex
Secondary Motor Cortex
Premotor Cortex

Cortical and Cerebral Regions

Cerebral Cortex Regions
Cerebellar and Brainstem Regions

Motor Cortex

Somatosensory Association Cortex
Visual Association Cortex

Auditory Association Area

Gyrus
Sulcus
Primary Visual Cortex
Extrastriate Body Area
Fusiform Body Area
Extrastriate Cortex
Lateral Inferior Prefrontal Cortex
Dorsal Posterior Parietal Cortex
Ventral Posterior Parietal Cortex
Dorsal Anterior Cingulate Cortex
Orbital Prefrontal Cortex
Ventromedial Prefrontal Cortex
Inferior Parietal Lobule
Supramarginal Gyrus
Angular Gyrus
Cuneus
Precuneus
Superior Parietal Lobule
Intraparietal Sulcus
Frontal Eye Fields

Brodmann Areas

Brodmann Area 6
Brodmann Area 8
Brodmann Area 17
Brodmann Area 18
Brodmann Area 19
Brodmann Area 5
Brodmann Area 7
Brodmann Area 39
Brodmann Area 40
Brodmann Area 41
Brodmann Area 42
Brodmann Area 22
Brodmann Area 21
Brodmann Area 20
Brodmann Area 37
Brodmann Area 38

Ventricles and Associated Structures

Lateral Ventricles
Interventricular Foramen
Third Ventricle
Inferior Horn of the Lateral Ventricle
Body of Lateral Ventricle
Anterior Horn of Lateral Ventricle
Posterior Horn of Lateral Ventricle
Cerebral Aqueduct
Fourth Ventricle
Choroid Plexus
Central Canal of Spinal Cord

Commissures and Associated Structures

Corpus Callosum
Column of the Fornix
Anterior Commissure
Posterior Commissure

Limbic System Structures

Hippocampus
Amygdala
Cingulate Gyrus
Fornix
Mammillary Body
Septal Nuclei
Parahippocampal Gyrus
Entorhinal Cortex

Other Brainstem and Associated Nuclei:

Midbrain
Superior Colliculus
Inferior Colliculus
Pons
Medulla Oblongata
Crus Cerebri
Cerebral Peduncle
Red Nucleus
Ventral Tegmental Area
Substantia Nigra
Oculomotor Nerve
Trochlear Nerve
Decussation of Superior Cerebellar Peduncle
Brachium of Inferior Colliculus
Brachium of Superior Colliculus
Interstitial Nucleus of Cajal
Basilar Pons
Pontine Tegmentum
Pontine Nuclei
Mesencephalic Nucleus of Trigeminal Nerve
Medial Lemniscus
Trapezoid Body
Superior Olivary Complex
Cochlear Nucleus
Facial Motor Nucleus
Abducens Nucleus
Medial Longitudinal Fasciculus
Nucleus of the Lateral Lemniscus
Nucleus of the Solitary Tract
Middle Cerebellar Peduncle
Corticospinal Tract
Corticopontine Tract
Spinothalamic Tract
Spinal Lemniscus
Reticular Formation
Paramedian Pontine Reticular Formation
Raphe Nuclei
Nucleus Ambiguus
Dorsal Respiratory Group
Ventral Respiratory Group
Pre-Bötzinger Complex
Hypoglossal Nucleus
Nucleus Gracilis
Nucleus Cuneatus
Solitary Nucleus
Spinal Trigeminal Nucleus

Basal Ganglia and Associated Structures:

Caudate Nucleus
Putamen
Globus Pallidus
Striatum
Thalamus
Subthalamus

Neural Coverings and Connective Tissue:

Epineurium
Perineurium
Endoneurium
Meninges
Dura Mater
Arachnoid Mater
Pia Mater

Limbic System and Associated Structures:

Hippocampus
Amygdala
Cingulate Gyrus
Fornix
Mammillary Body
Septal Nuclei
Parahippocampal Gyrus
Entorhinal Cortex

Ventricular System and Associated Structures:

Lateral Ventricles
Interventricular Foramen
Third Ventricle
Cerebral Aqueduct
Fourth Ventricle
Choroid Plexus
Pineal Gland
Posterior Pituitary
Anterior Pituitary
Optic Chiasm
Infundibulum

White Matter Tracts and Associated Structures:

Mammillothalamic Tract
Medial Forebrain Bundle
Corpus Callosum
Column of the Fornix
Anterior Commissure
Posterior Commissure
Corticospinal Tract

Spinal Cord and Associated Structures:

Spinal Cord
Dorsal Root
Ventral Root
Dorsal Root Ganglion
Spinothalamic Tract
Dorsal Column-Medial Lemniscus Pathway

Peripheral Nervous System:

Epineurium
Perineurium
Endoneurium

Meninges and Protective Layers:

Meninges
Dura Mater

Cerebrovascular System:

Circle of Willis
Carotid Sinus
Cerebral Aqueduct
Cerebral Sinuses
Arachnoid Granulation

Ventricular System:

Lateral Ventricles
Third Ventricle
Fourth Ventricle
Choroid Plexus

Corpus Callosum and Associated Structures:

Corpus Callosum
Genu of Corpus Callosum
Splenium of Corpus Callosum

Meninges and Coverings:

Meninges
Dura Mater
Arachnoid Mater
Pia Mater
Arachnoid Granulations
Arachnoid Granulation
Cerebral Sinuses
Choroid Plexus

Peripheral Neural Structures and Layers:

Epineurium
Perineurium
Endoneurium

Limbic System and Associated Structures:

Limbic System
Amygdala
Hippocampus
Fornix
Mammillary Body
Cingulate Gyrus
Parahippocampal Gyrus
Entorhinal Cortex

Blood Supply and Vascular Structures:

Circle of Willis
Carotid Sinus
Cavernous Sinus
Tuberculum Sellae

Neural Pathways:

Corticospinal Tract
Corticopontine Tract
Spinothalamic Tract
Trigeminothalamic Tract
Trigeminocerebellar Tract
Medial Lemniscus

Limbic System and Associated Structures:

Limbic System
Hippocampus
Amygdala
Cingulate Gyrus
Septal Nuclei
Fornix
Mammillary Body

Other Notable Structures (Continued):

Pineal Gland
Cavernous Sinus
Substantia Innominata
Subcommissural Organ
Septum Pellucidum
Lamina Terminalis
Tela Choroidea
Optic Chiasm
Infundibulum
Posterior Pituitary
Anterior Pituitary
Thalamus
Subthalamus
Periaqueductal Gray
Reticular Formation
Pineal Gland
Arachnoid Mater
Pia Mater

https://reasonandscience.catsboard.com

305Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 3:27 pm

Otangelo


Admin

Cerebellar and Brainstem Regions

Cerebellar Regions

Anterior Lobe
Posterior Lobe
Flocculonodular Lobe
Vermis
Cerebellar Tonsil
Cerebellar Cortex
Deep Cerebellar Nuclei

Cerebellar Cell Types and Subtypes:

Neurons
   Purkinje Cells
     - Standard Purkinje cells
     - Zebrin II-positive and Zebrin II-negative subtypes
   Granule Cells
   Golgi Cells
   Basket Cells
   Stellate Cells
   Lugaro Cells
   Unipolar Brush Cells

Glial Cells
   Bergmann Glia
   Astrocytes
   Oligodendrocytes
   Microglia

Fibers
   Mossy Fibers
   Climbing Fibers
   Parallel fibers (axons of the Granule Cells)

Interneurons
   Golgi cells
   Basket cells
   Stellate cells

Brainstem Regions

Midbrain
Tectum
Tegmentum
Crus Cerebri
Pons
Basilar Part of the Pons
Pontine Tegmentum
Pontine Nuclei
Medulla Oblongata

Brainstem Cell Types and Subtypes

Neurons
   Motor Neurons
     - Lower motor neurons
     - Cranial nerve nuclei neurons
   Interneurons
   Projection neurons
   Relay neurons

Glial Cells
   Astrocytes
   Oligodendrocytes
   Microglia
   Ependymal Cells

Fibers
   Ascending and Descending Tracts
     - Corticospinal tracts
     - Reticulospinal tracts
     - Rubrospinal tracts
     - Spinothalamic tracts

Interneurons
   Local circuit interneurons
   Relay interneurons

https://reasonandscience.catsboard.com

306Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 3:42 pm

Otangelo


Admin

//// give first an overview, and then list the cell types it contains, and explain the connections etc. Has here, in BBcode, the exact same format:

The Fastigial Nucleus is the most medially positioned nucleus among the deep cerebellar nuclei. Located within the white matter core of the cerebellum, its name is derived from the Latin word "fastigium," meaning "summit," reflecting its location near the cerebellar roof.

Anatomical Connections: The fastigial nucleus receives afferent (incoming) connections mainly from the Purkinje cells of the cerebellar vermis. It sends efferent (outgoing) projections to several areas, including the vestibular nuclei, the reticular formation, and, through the superior cerebellar peduncle, to the thalamus and then the cerebral cortex.
Functional Role: The fastigial nucleus is primarily involved in the control of axial and proximal limb muscles. As a result, it plays a critical role in maintaining balance and an upright posture. When there's a need for modifications in posture or balance, such as when walking on an uneven surface or making sudden movements, the fastigial nucleus integrates sensory feedback with motor commands to make the necessary adjustments.
Interactions with Other Systems: The fastigial nucleus communicates with other motor and sensory systems to generate a comprehensive motor plan. For instance, when planning a movement like reaching out for an object, the visual and spatial information about the object's location is integrated with proprioceptive feedback (information about body position) to coordinate the movement effectively.

The Fastigial nucleus, as a deep cerebellar nucleus, has a somewhat different cellular composition compared to the cerebellar cortex. The deep cerebellar nuclei (which include the fastigial nucleus) primarily consist of output neurons from the cerebellum to other parts of the brain. These large projection neurons, known as glutamatergic projection neurons, are the primary cell type found in these nuclei. However, within these nuclei, you'll also find a variety of interneurons, which provide inhibitory feedback within the nucleus. These could be GABAergic neurons. There are also astrocytes and microglia present, which are common to many regions of the brain.




Anterior Lobe of Cerebellum

The Anterior Lobe of the Cerebellum is primarily involved in regulating motor movements, particularly the coordination of limb movements. The cellular architecture and their connections within this lobe play a crucial role in this regulation.

Purkinje Cells:
Connections: These cells receive two major types of input: from climbing fibers (originating mainly from the inferior olivary nucleus) and from parallel fibers (the axons of granule cells). Each Purkinje cell receives input from only one climbing fiber, but this single input makes multiple contacts with the Purkinje cell.
Function & Role: Purkinje cells are the primary output neurons of the cerebellar cortex. Their axons project to the deep cerebellar nuclei and emit inhibitory signals. The balance between the excitatory inputs from climbing and parallel fibers and the intrinsic inhibitory nature of Purkinje cells helps fine-tune motor coordination.


Cerebellar Cell Types and Subtypes:

Neurons
   Purkinje Cells
     - Standard Purkinje cells
     - Zebrin II-positive and Zebrin II-negative subtypes
   Granule Cells
   Golgi Cells
   Basket Cells
   Stellate Cells
   Lugaro Cells
   Unipolar Brush Cells

Glial Cells
   Bergmann Glia
   Astrocytes
   Oligodendrocytes
   Microglia

Fibers
   Mossy Fibers
   Climbing Fibers
   Parallel fibers (axons of the Granule Cells)

Interneurons
   Golgi cells
   Basket cells
   Stellate cells



Last edited by Otangelo on Fri Oct 06, 2023 10:32 am; edited 1 time in total

https://reasonandscience.catsboard.com

307Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 04, 2023 3:43 pm

Otangelo


Admin

///// I dont want points, but a Continuous narrative format without using repetitive or flowery language. Please provide a scientific explanation.  a factual and precise account. an academic-style write-up.  I want an “objective,” “formal,” or “scientific” tone for a straightforward and factual text. In bbcode  When you finish the text, never write: in summary. Just summarize, without mentioning it.

https://reasonandscience.catsboard.com

308Perguntas .... - Page 13 Empty Re: Perguntas .... Fri Oct 06, 2023 6:16 pm

Otangelo


Admin

Gene Expression and Regulation in LUCA

To understand the earliest life forms, it's essential to grasp how genes were regulated and expressed in LUCA. Here are some fundamental elements and their roles.

Gene Regulatory Network (GRN): This is the interconnected system of genes and their products that govern when and which genes are expressed.
Transcription Factors (TFs): These proteins influence the transcription of specific genes by assisting or hindering RNA polymerase's DNA binding.
Sigma Factors: These proteins help RNA polymerase identify promoter sequences, especially in prokaryotes.
Epigenetic Factors: Molecular changes on DNA or associated proteins that can modify gene activity without changing the DNA sequence.
Small RNAs (sRNAs): Non-coding RNA molecules that play various roles in RNA silencing and post-transcriptional regulation of gene expression.
Operons: A functioning unit of DNA that contains a cluster of genes under a single promoter's control.
Repressor and Activator Proteins: These proteins can inhibit or promote transcription based on environmental or internal cues by binding to DNA.
DNA Methylation: The addition of methyl groups to the DNA molecule can modify gene activity without changing the DNA sequence.
DNA Binding Domains: These are specific protein regions that enable them to bind to DNA, crucial for transcriptional regulation.
Two-component Signaling Systems: They consist of a sensor kinase and a response regulator, enabling cells to sense and respond to environmental shifts, predominantly in prokaryotes.
Co-factors and Metabolites: These small molecules can influence transcription by binding to particular proteins, affecting the transcriptional outcome.


References

 Jacob, F., & Monod, J. (1961). Genetic regulatory mechanisms in the synthesis of proteins. Journal of Molecular Biology, 3(3), 318-356. Link. (This groundbreaking paper introduced the concept of operons, discussing their role in the coordinated expression of genes.)
 Ptashne, M., Jeffrey, A., Johnson, A. D., Maurer, R., Meyer, B. J., Pabo, C. O., ... & Sauer, R. T. (1980). How the λ repressor and cro work. Cell, 19(1), 1-11. Link. (A seminal paper discussing the role of repressors in regulating gene expression, using the lambda phage as a model.)
 Winge, D. R., & Roberts, J. M. (1992). Cooperativity in transcription factor binding to the regulatory elements of the yeast metallothionein gene. Journal of Biological Chemistry, 267(18), 12744-12748. Link. (Investigates the role of cooperativity among transcription factors in gene regulation.)
 Stock, A. M., Robinson, V. L., & Goudreau, P. N. (2000). Two-component signal transduction. Annual Review of Biochemistry, 69(1), 183-215. Link. (A detailed overview of the two-component signaling system, especially common in prokaryotes.)
 Goll, M. G., & Bestor, T. H. (2005). Eukaryotic cytosine methyltransferases. Annual Review of Biochemistry, 74(1), 481-514. Link. (This review delves deep into the role of DNA methylation in gene regulation, exploring its mechanisms and significance.)
 Davidson, E. H. (2010). Emerging properties of animal gene regulatory networks. Nature, 468(7326), 911-920. Link. (Provides insights into the complexity of gene regulatory networks, discussing their evolution and implications.)
 Storz, G., Vogel, J., & Wassarman, K. M. (2011). Regulation by small RNAs in bacteria: expanding frontiers. Molecular Cell, 43(6), 880-891. Link. (A comprehensive review on the roles of small RNAs in bacterial gene regulation.)
 Smith, Z. D., & Meissner, A. (2013). DNA methylation: roles in mammalian development. Nature Reviews Genetics, 14(3), 204-220. Link. (Examines the significance of DNA methylation in development, shedding light on its wider implications in gene expression.)
 Gagler, D., Karas, B., Kempes, C., Goldman, A., Kim, H., & Walker, S. (2021). Scaling laws in enzyme function reveal a new kind of biochemical universality. Proceedings of the National Academy of Sciences of the United States of America, 119. Link.

https://reasonandscience.catsboard.com

309Perguntas .... - Page 13 Empty Re: Perguntas .... Fri Oct 06, 2023 6:25 pm

Otangelo


Admin

The Last Universal Common Ancestors Proteome


Gene Expression and Regulation in LUCA

5-Aminolevulinate synthase (ALAS):  EC: 2.3.1.37 
Porphobilinogen synthase (PBGS): EC: 2.3.1.37 
Porphobilinogen deaminase: EC: 2.5.1.61 
Uroporphyrinogen III synthase: EC: 4.2.1.75 
Uroporphyrinogen III decarboxylase: EC: 4.1.1.37 
Coproporphyrinogen III oxidase: EC: 1.3.3.3 
Protoporphyrinogen IX oxidase: EC: 1.3.3.4 
Ferrochelatase: EC: 4.99.1.1 


Manganese transporters

Manganese transport protein
Manganese-dependent superoxide dismutase (Mn-SOD): EC: 1.15.1.1 

Molybdenum/Tungsten (Mo/W) Cofactors

Molybdenum cofactor biosynthesis protein A (MoaA): EC: 1.14.99.53 
Molybdenum cofactor biosynthesis protein C (MoaC): EC: 4.6.1.17 
Molybdopterin converting factor (MoaD/MoaE)
Molybdenum cofactor biosynthesis protein B (MoaB)

Nickel (Ni) Centers

Hydrogenase nickel incorporation protein HypB: EC: 3.6.1.15
Hydrogenase maturation protein HypA
UreE, UreG, UreF, UreH

Zinc (Zn) Centers

ZnuA - Part of the ZnuABC system
Zur - Zinc uptake regulator
Zinc-transporting ATPase (ZntA): EC: 7.2.2.10

Nucleotide Synthesis and Salvage

Ribose-phosphate diphosphokinase (EC 2.7.6.1): EC: 2.7.6.1 
Amidophosphoribosyl transferase (GPAT) (EC 2.4.2.14): EC: 2.4.2.14 
Glycinamide ribotide (GAR) transformylase (GART) (EC 2.1.2.2): EC: 2.1.2.2 
Formylglycinamide ribotide (FGAR) amidotransferase (GART) (EC 3.5.4.10): EC: 3.5.4.10 
Formylglycinamidine ribotide (FGAM) synthetase (GART) (EC 6.3.5.3): EC: 6.3.5.3 
5-aminoimidazole ribotide (AIR) carboxylase (PurK) (EC 4.1.1.21): EC: 4.1.1.21 
5-aminoimidazole-4-(N-succinylocarboxamide) ribotide (SACAIR) synthetase (PurE) (EC 6.3.2.6): EC: 6.3.2.6 
Carboxyaminoimidazole ribotide (CAIR) mutase (PurK) (EC 5.4.99.18): EC: 5.4.99.18 
5-aminoimidazole-4-carboxamide ribotide (AICAR) transformylase (PurN) (EC 2.1.2.3): EC: 2.1.2.3 
5-formaminoimidazole-4-carboxamide ribotide (FAICAR) cyclase (PurM) (EC 3.5.4.21): EC: 3.5.4.21 
IMP cyclohydrolase (PurH) (EC 3.5.4.10): EC: 3.5.4.10 


Carbamoyl phosphate synthetase II (CPSII): EC: 6.3.5.5 
Aspartate transcarbamoylase (ATCase): EC: 2.1.3.2 
Dihydroorotase (DHOase): EC: 3.5.2.3 
Dihydroorotate dehydrogenase (DHODH): EC: 1.3.5.2 
Orotate phosphoribosyltransferase (OPRT): EC: 2.4.2.10 
Orotidine 5'-monophosphate decarboxylase (OMPDC): EC: 4.1.1.23 
Nucleoside monophosphate kinase (UMP/CMP kinase): EC: 2.7.4.14 
Nucleoside diphosphate kinase (NDK): EC: 2.7.4.6 
CTP synthetase (CTPS): EC: 6.3.4.2 

Adenine (A) Ribonucleotide Biosynthesis

Phosphoribosylaminoimidazole carboxylase (PurE): EC: 4.1.1.21 
Adenylosuccinate synthetase (PurA): EC: 6.3.4.4 
Adenylosuccinate lyase (PurB): EC: 4.3.2.2 

Guanine (G) Ribonucleotide Biosynthesis

IMP dehydrogenase (IMPDH): EC: 1.1.1.205 
GMP synthetase (GuaA): EC: 6.3.5.2 

Uracil (U) Ribonucleotide Biosynthesis (leading to UMP)

Carbamoyl phosphate synthetase II (CPSII): EC: 6.3.4.16 
Aspartate transcarbamoylase (ATCase): EC: 2.1.3.2 
Dihydroorotase (DHOase): EC: 3.5.2.3 
Dihydroorotate dehydrogenase (DHODH): EC: 1.3.3.1 
Orotate phosphoribosyltransferase (OPRT): EC: 2.4.2.10 
Orotidine 5'-monophosphate decarboxylase (OMPDC): EC: 4.1.1.23 

Cytosine (C) Ribonucleotide Biosynthesis (leading to CTP from UTP)

Nucleoside monophosphate kinase (UMP/CMP kinase): EC: 2.7.4.14 
Nucleoside diphosphate kinase (NDK): EC: 2.7.4.6 
CTP synthetase (CTPS): EC: 6.3.4.2 

Thymine (T) Deoxyribonucleotide Biosynthesis (leading to dTMP from dUMP):

Ribonucleotide reductase (RNR): EC: 1.17.4.1 
Dihydrofolate reductase (DHFR): EC: 1.5.1.3 
Thymidylate synthase (TYMS or TS): EC: 2.1.1.45 

Deoxynucleotide Biosynthesis:

ADP to dADP: EC: 1.17.4.1
CDP to dCDP: EC: 1.17.4.1 
GDP to dGDP: EC: 1.17.4.1
UDP to dUDP: EC: 1.17.4.1 

NDK: EC: 2.7.4.6 
NDK: EC: 2.7.4.6 
NDK: EC: 2.7.4.6 
NDK: EC: 2.7.4.6 

dUTPase (dUTP pyrophosphatase): EC: 3.6.1.23 

ATP-binding cassette (ABC) transporters
Adenine phosphoribosyltransferase (APRT)
Hypoxanthine-guanine phosphoribosyltransferase (HGPRT): EC: 2.4.2.8 
Glutamine transporters
Tetrahydrofolate (THF) and its derivatives
S-adenosylmethionine (SAM) transporters
Amino acid synthetases
Nucleotidases
Dihydrofolate reductase: EC: 1.5.1.3 
Purine Transporters
Pyrimidine Transporters
Phosphate Transporters
Ribose/Deoxyribose Transporters

Magnesium transporters 

Magnesium transporters (Mgt)
CorA
Magnesium efflux systems
Magnesium-binding proteins
Magnesium-sensing proteins
Enzymatic cofactors
RNA structures

Amino Acid Transporters in LUCA

Amino Acid Antiporters
Amino Acid/H+ Symporters
ATP-binding Cassette (ABC) Amino Acid Transporters
Passive Diffusion

Nucleotide Transporters in LUCA

Nucleotide Antiporters
Nucleotide/H+ Symporters
ATP-binding Cassette (ABC) Nucleotide Transporters
Nucleotide-specific Channels
Vesicular Transport
Nucleoside Transporters
P4-ATPases
Facilitated Diffusion Nucleotide Transporters

Nucleoside Transporters in LUCA

Concentrative Nucleoside Transporters (CNTs)
Equilibrative Nucleoside Transporters (ENTs)
ATP-binding Cassette (ABC) Nucleoside Transporters
Nucleoside/H+ Symporters
Nucleoside Antiporters
Vesicular Nucleoside Transport
Specific Channel-formed Nucleoside Transporters
Nucleoside-specific Pore-forming Proteins

Phosphate Transporters in LUCA

PiT Family Transporters
Pst Phosphate Transport System
Pho89 Sodium-Phosphate Transporter
Low Affinity Phosphate Transporters
High Affinity Phosphate Transporters 
Phosphate Antiporters 
Phosphate/H+ Symporters 
Vesicular Phosphate Transport 
Passive Phosphate Channels 

Folate Transporters in LUCA

Folate-Binding Protein (FBP) Transporters
Proton-Coupled Folate Transporter (PCFT)

Reduced Folate Carrier (RFC)
Multidrug Resistance Protein (MRP) Transporters

Folate Receptors (FRs)
ABC Transporters


SAM Transporters in LUCA

SAM Transporter (SAMT)
ABC Transporters
Solute Carrier Family Transporters
Multidrug Resistance Proteins (MRPs)
Vesicular Transport Mechanisms

Carbon Source Transporters in LUCA

Glucose/Galactose Transporter (GLUT)
ABC Glucose Transporters
Hexose Transporter (HXT)

Amino Acid Precursors for Nucleotide Synthesis Transporters in LUCA

Glutamine Transporters
Aspartate Transporters
Glycine Transporters (GlyT)

Co-factor Transporters for Nucleotide Synthesis in LUCA

Vitamin B6 Transporters
Tetrahydrofolate (THF) Transporters

Ion Transporters in LUCA with Relevance to Nucleotide Synthesis

Potassium (K+) Transporters
Zinc (Zn2+) Transporters

RNA Recycling


RNA 3'-terminal phosphate cyclase (EC 3.1.3.43) 

Ribonucleases:

RNase II: EC: 3.1.26.4 
RNase R: EC: 3.1.26.3 


Exoribonucleases

Exoribonuclease II: EC: 3.1.13.4 Degrades RNA from the 3' end.
Exoribonuclease III: EC: 3.1.13.1 Involved in RNA degradation.

DNA Recycling

Polynucleotide 5'-phosphataseEC: 3.1.4.47 Hydrolyzes the 5'-phosphate of single-stranded DNA.

Deoxyribonucleases

Deoxyribonuclease IEC: 3.1.11.2 

Exonucleases

Exonuclease III: EC: 3.1.11.1 Involved in DNA degradation.
Exonuclease I: EC: 3.1.11.1 Degrades single-stranded DNA from the 3' end.

Endonucleases:

Endonuclease IVEC: 3.1.21.2 


Serine Synthesis:

Phosphoserine phosphatase: EC: 3.1.3.3 
Phosphoserine aminotransferase: EC: 2.6.1.52

Glycine Synthesis 

Serine hydroxymethyltransferase: EC: 2.1.2.1 
Glycine decarboxylase (P Protein): EC: 1.4.4.2 
Aminomethyltransferase (T Protein): EC: 2.1.2.10 
Glycine cleavage system H protein (H Protein): 
Dihydrolipoyl dehydrogenase (L Protein): EC: 1.8.1.4 

Cysteine Metabolism

Serine O-acetyltransferase: EC: 2.3.1.30 
Cysteine synthase: EC: 2.5.1.47 
Methionine adenosyltransferase: EC: 2.5.1.6 
S-Adenosylhomocysteine hydrolase: EC: 3.3.1.1 
Cystathionine gamma-synthase: EC: 2.5.1.48 

Alanine Metabolism

Aspartate 4-decarboxylase: EC: 4.1.1.12 
Alanine transaminase: EC: 2.6.1.2 
Alanine-glyoxylate transaminase: EC: 2.6.1.44 
Alanine dehydrogenase: EC: 1.4.1.1 
Alanine racemase: EC: 5.1.1.1 

Valine biosynthesis

Acetolactate synthase: EC: 2.2.1.6 
Acetohydroxy acid isomeroreductase: EC: 1.1.1.86 
Dihydroxyacid dehydratase: EC: 4.2.1.9 
Branched-chain amino acid aminotransferase: EC: 2.6.1.42 

Leucine Biosynthesis in Bacteria (precursors same as Valine)

Acetolactate synthase: EC: 2.2.1.6 
Dihydroxy-acid dehydratase: EC: 4.2.1.9 
3-isopropylmalate synthase: EC: 2.3.3.13 
3-isopropylmalate dehydratase: EC: 4.2.1.33 
3-isopropylmalate dehydrogenase: EC: 1.1.1.85 
Branched-chain amino acid aminotransferase: EC: 2.6.1.42 

Isoleucine Metabolism (from Threonine):

Threonine deaminase: EC: 4.3.1.19 
3-methyl-2-oxobutanoate hydroxymethyltransferase: EC: 2.1.2.11 
3-isopropylmalate dehydratase: EC: 4.2.1.33 
3-isopropylmalate dehydrogenase: EC: 1.1.1.85 

Histidine Synthesis

Phosphoribosylamine--glycine ligase: EC: 6.3.4.13 
Phosphoribosylformylglycinamidine synthase: EC: 6.3.5.3 
Phosphoribosylformylglycinamidine cyclo-ligase: EC: 6.3.3.1 
Phosphoribosylformimino-5-amino-1-(5-phosphoribosyl)imidazolecarboxamide isomerase (EC 5.3.1.16)
Imidazoleglycerol-phosphate synthase (EC 4.1.3.15)
Imidazoleglycerol-phosphate hydrolase (EC 3.13.1.5)
Histidinol-phosphate aminotransferase (EC 2.6.1.9)
Histidinol-phosphate phosphatase (EC 3.1.3.15)
Histidinol dehydrogenase: EC: 1.1.1.23 
Histidine ammonia-lyase: EC: 4.3.1.3 

Phenylalanine/Tyrosine Synthesis pathway

Chorismate mutase: EC: 5.4.99.5 

For Tyrosine synthesis

Prephenate dehydrogenase: EC: 1.3.1.12 
4-Hydroxyphenylpyruvate dioxygenase: EC: 1.13.11.27 
Homogentisate 1,2-dioxygenase: EC: 1.13.11.5 

For Phenylalanine synthesis

Prephenate aminotransferase: EC: 2.6.1.78 
Arogenate dehydratase: EC: 4.2.1.91 

Tryptophan Synthesis

Chorismate pyruvate-lyase: EC: 4.2.99.21 
Anthranilate phosphoribosyltransferase: EC: 2.4.2.18 
Phosphoribosylanthranilate isomerase: EC: 5.3.1.24 
Indole-3-glycerol-phosphate synthase: EC: 4.1.1.48 
Tryptophan synthase: EC: 4.2.1.20 

Aspartate Metabolism

Aspartate transaminase: EC: 2.6.1.1 
Aspartate carbamoyltransferase: EC: 2.1.3.2 
Aspartokinase: EC: 2.7.2.4 
Adenylosuccinate synthase: EC: 6.3.4.4 

Asparagine Metabolism

Asparagine synthetase: EC: 6.3.5.4 
Asparaginase: EC: 3.5.1.1 
Asparagine aminotransferase: EC: 2.6.1.14 

Methionine Metabolism

Homoserine dehydrogenase: EC: 1.1.1.3 
O-succinylhomoserine (thiol)-lyase: EC: 2.5.1.48 
Cystathionine beta-lyase: EC: 4.4.1.8
Methionine synthase: EC: 2.1.1.13 
Methylthiotransferase: EC: 2.8.4.4 

Lysine Biosynthesis

Dihydrodipicolinate synthase: EC: 4.2.1.52 
Dihydrodipicolinate reductase: EC: 1.3.1.26 
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase: EC: 2.3.1.117 
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase: EC: 2.3.1.89 
Diaminopimelate reductase: EC: 1.3.1.26 
Diaminopimelate epimerase: EC: 5.1.1.7 
Diaminopimelate decarboxylase: EC: 4.1.1.20 

Threonine Metabolism

Aspartokinase: EC: 2.7.2.4 
Aspartate-semialdehyde dehydrogenase: EC: 1.2.1.11 
Homoserine dehydrogenase: EC: 1.1.1.3 
Homoserine kinase: EC: 2.7.1.39 
Threonine synthase: EC: 4.2.3.1 

Glutamine/Glutamate Synthesis

Glutamate dehydrogenase (NAD+): EC: 1.4.1.2 
Glutamate dehydrogenase (NADP+): EC: 1.4.1.4 
Glutamate 5-kinase: EC: 2.7.2.11 
Glutamine synthetase: EC: 6.3.1.2 
Glutamine-dependent NAD+ synthetase: EC: 6.3.5.1 

Arginine/Ornithine Synthesis

N-acetylglutamate synthase: EC: 2.3.1.1 
N-acetylglutamate kinase: EC: 2.7.2.8 
N-acetyl-gamma-glutamyl-phosphate reductase: EC: 1.2.1.38 
Acetylornithine aminotransferase: EC: 2.6.1.11 
Ornithine carbamoyltransferase: EC: 2.1.3.3 
Argininosuccinate synthase: EC: 6.3.4.5 
Argininosuccinate lyase: EC: 4.3.2.1 
Arginine Metabolism in Prokaryotes

L-Glutamate
L-Citrulline
Ornithine:

Proline Metabolism in Prokaryotes

L-Glutamate
Ornithine
L-Glutamate-5-semialdehyde
Ornithine carbamoyltransferase: EC: 2.1.3.3 
Ornithine decarboxylase: EC: 4.1.1.17 
Acetylornithine deacetylase: EC: 3.5.1.16 
Proline dehydrogenase: EC: 1.5.5.2 
Pyrroline-5-carboxylate reductase: EC: 1.5.1.2

Nicotinate and Nicotinamide Metabolism

Nicotinamidase: EC: 3.5.1.19 
Nicotinate phosphoribosyltransferase: EC: 2.4.2.11 
Quinolinate phosphoribosyltransferase: EC: 2.4.2.19 
Nicotinate-nucleotide pyrophosphorylase [carboxylating]: EC: 2.4.2.19 
Nicotinamide phosphoribosyltransferase: EC: 2.4.2.12 
Nicotinamide riboside kinase: EC: 2.7.1.173 
Nicotinate-nucleotide adenylyltransferase: EC: 2.7.7.18 
NAD+ synthase: EC: 6.3.5.1 
NR 5'-phosphate adenylyltransferase: EC: 2.7.7.1 
Nicotinate dehydrogenase: EC: 1.17.1.5 
NADH pyrophosphatase: EC: 3.6.1.22 

Amino Acid degradation


Alanine dehydrogenaseEC: 1.4.1.1 
ArginaseEC: 3.5.3.1 
AsparaginaseEC: 3.5.1.1 
Asparagine aminotransferaseEC: 2.6.1.14 
Aspartate transaminaseEC: 2.6.1.1
Aspartate carbamoyltransferaseEC: 2.1.3.2
Aspartokinase (EC 2.7.2.4)  
O-succinylhomoserine (thiol)-lyase: EC: 2.5.1.48 
Glutamate synthaseEC: 1.4.1.13 
GlutaminaseEC: 3.5.1.2 
Glutamate dehydrogenaseEC: 1.4.1.3 
Glutaminase (EC 3.5.1.2) 
Glycine cleavage system: EC: 1.4.4.2, EC: 1.8.1.4, EC: 2.1.2.10 
Serine hydroxymethyltransferase: EC: 2.1.2.1 
Histidinol-phosphate phosphatase (EC 3.1.3.15)
Histidinol dehydrogenase (EC 1.1.1.23)
Histidine ammonia-lyase (EC 4.3.1.3)
Threonine deaminase (EC 4.3.1.19)
3-isopropylmalate dehydratase: EC: 4.2.1.33 
3-isopropylmalate dehydrogenase: EC: 1.1.1.85 
Diaminopimelate epimerase: EC: 5.1.1.7 
Diaminopimelate decarboxylase: EC: 4.1.1.20 
Homoserine dehydrogenase: EC: 1.1.1.3 
Arogenate dehydratase: EC: 4.2.1.91 
Pyrroline-5-carboxylate reductase: EC: 1.5.1.2 
Proline dehydrogenase: EC: 1.5.5.2 
Serine hydroxymethyltransferase: EC: 2.1.2.1 
Tryptophanase: EC: 4.1.99.1 
Tyrosine phenol-lyase: EC: 4.1.99.2 



Regulatory Enzymes and Proteins in Amino Acid synthesis

Amino Acid Transaminases

Methionine Transaminase: EC: 2.6.1.40 
Alanine Transaminase: EC: 2.6.1.2 
Aspartate Transaminase: EC: 2.6.1.1 
Glutamate-pyruvate Transaminase: EC: 2.6.1.2 
Glutamate-oxaloacetate Transaminase: EC: 2.6.1.1 
Phenylalanine Transaminase: EC: 2.6.1.79 
Tyrosine Transaminase: EC: 2.6.1.5
Tryptophan Transaminase: EC: 2.6.1.7 
Glutamate--pyruvate Transaminase: EC: 2.6.1.2 
Alanine--glyoxylate Transaminase: EC: 2.6.1.44
Serine--glyoxylate Transaminase: EC: 2.6.1.43 
Cysteine--glyoxylate Transaminase: EC: 2.6.1.23 

Amino Acid Dehydrogenases:

Alanine Dehydrogenase: EC: 1.4.1.1 
Glutamate Dehydrogenase: EC: 1.4.1.3 
Tyrosine Dehydrogenase: 
Tryptophan Dehydrogenase: 
Lysine Dehydrogenase: 
Proline Dehydrogenase: 
Phenylalanine Dehydrogenase:
Leucine Dehydrogenase: 
Arginase: EC: 3.5.3.1 
Arginine Deiminase: 
Glutamine Synthetase: EC: 6.3.1.2 
Alanine--glyoxylate Transaminase 2
Alanine--glyoxylate Transaminase 1

Amino Acid Kinases:

Alanine Kinase: EC: 2.7.1.29 
Aspartate Kinase: EC: 2.7.2.4 
Glutamate Kinase: EC: 2.7.2.11 
Phenylalanine Kinase: EC: 2.7.1.40 
Tyrosine Kinase: EC: 2.7.1.40 
Isoleucine Kinase: EC: 2.7.1.40 
Leucine Kinase: EC: 2.7.1.40 
Arginine Kinase: EC: 2.7.3.3 
Methionine Kinase: EC: 2.7.1.40 
Proline Kinase: [EC: 2.7.2.11]
Tryptophan Kinase: [EC: 2.7.1.40]
Cysteine Kinase: [EC: 2.7.1.40]
Glycine Kinase: [EC: 2.7.1.40]
Histidine Kinase: [EC: 2.7.13.3]
Serine Kinase: [EC: 2.7.1.40]
Threonine Kinase: [EC: 2.7.1.40]
Lysine Kinase: [EC: 2.7.1.40]

Amino Acid Transporters:
Alanine Transporter
Aspartate Transporter
Glutamate Transporter
Phenylalanine Transporter
Tyrosine Transporter
Isoleucine Transporter
Leucine Transporter
Arginine Transporter
Methionine Transporter
Proline Transporter
Tryptophan Transporter
Cysteine Transporter
Lysine Transporter
Histidine Transporter
Serine Transporter
Threonine Transporter
Glycine Transporter
Valine Transporter
Glutamine Transporter
Serine/Glycine Transporter
Cystine Transporter
Glutamate/Glutamine Transporter
Ornithine Transporter
Diaminopimelate Transporter


Fatty Acid and Phospholipid Synthesis in LUCA

Initiation of Fatty Acid Synthesis:
- Acetyl-CoA carboxylase: EC: 6.4.1.2
- Malonyl-CoA-acyl carrier protein transacylase: EC: 2.3.1.39

Elongation through Fatty Acid Synthase Complex:
- Fatty Acid Synthase - Malonyl/Acetyltransferase: EC: 2.3.1.39
- Fatty Acid Synthase - 3-ketoacyl-ACP synthase: EC: 2.3.1.41
- Fatty Acid Synthase - 3-ketoacyl-ACP reductase: EC: 1.1.1.100
- Fatty Acid Synthase - 3-hydroxyacyl-ACP dehydratase: EC: 4.2.1.59
- Fatty Acid Synthase - Enoyl-ACP reductase: EC: 1.3.1.9

Termination and Modification:
- Fatty acid synthase: EC: 2.3.1.86
- Stearoyl-CoA desaturase: EC: 1.14.19.1

Fatty Acid Elongation (if needed):
- Enoyl-ACP reductase: EC: 1.3.1.9

Phospholipid Synthesis in LUCA:
- Glycerol-3-phosphate O-acyltransferase (GPAT): EC: 2.3.1.15
- Lysophosphatidic acid acyltransferase (LPAAT): EC: 2.3.1.51

Formation of phospholipid head groups:
- Phosphatidate cytidylyltransferase: EC: 2.7.7.41
- Ethanolaminephosphate cytidylyltransferase: EC: 2.7.7.14
- CDP-diacylglycerol—ethanolamine O-phosphatidyltransferase: EC: 2.7.8.1
- CDP-diacylglycerol—serine O-phosphatidyltransferase: EC: 2.7.8.8
- Phosphatidylserine decarboxylase: EC: 4.1.1.65

CDP-diacylglycerol pathway:
- Glycerol-3-phosphate O-acyltransferase: EC: 2.3.1.15
- 1-acylglycerol-3-phosphate O-acyltransferase: EC 2.3.1.51
- Phosphatidate cytidylyltransferase: EC: 2.7.7.41
- Phosphatidylglycerophosphate synthase: EC: 2.7.8.5
- Phosphatidylserine synthase: EC: 2.7.8.8
- Phosphatidylethanolamine synthase: EC: 2.7.8.1


Flippases (P-type ATPases)

ATP8A1
ATP8B1

Floppases (ABC Transporters)

ABCA1
ABCB1 (or MDR1/P-glycoprotein)

Uptake of Glycerol-3-phosphate (G3P) for the Glycerol Backbone:

GlpT (Glycerol-3-Phosphate Transporter)

Uptake of Fatty Acids or Precursors:

Fatty Acid Transport Proteins (FATPs)
ABC Transporters

Uptake of Phosphate for the Phospho-head Group:

Pst Phosphate Transport System
Pho89 Sodium-Phosphate Transporter

Uptake of Nucleotide Precursors for CDP-diacylglycerol Synthesis:

Nucleotide Transporters

Uptake of Amino Acids for the Phospholipid Head Group:

Serine Transporters
Ethanolamine Transporters

Phospholipid Degradation

Phospholipase A1 (PlaA)EC: 3.1.1.32
Phospholipase A2 (PlaB)EC: 3.1.1.4
Phospholipase C (Plc)EC: 3.1.4.3 
Phospholipase D (Pld)EC: 3.1.4.4 

Lipid Reuse and Recycling

Glycerophosphodiester phosphodiesterase (GlpQ)EC: 3.1.4.2

Conversion and Recycling of Head Groups

CDP-diacylglycerol-serine O-phosphatidyltransferase (PSS): EC: 2.7.7.15 
Phosphatidate phosphatase (PAP)EC: 3.1.3.4 
Diacylglycerol kinase (DGK)EC: 2.7.1.137 

Metabolites

Diacylglycerol
Phosphatidic acid
Glycerol-3-phosphate
CDP-diacylglycerol
Diacylglycerol

Two-component systems (TCS):

Histidine kinase (HK)EC: 2.7.13.3 
Response regulator (RR): EC: 2.7.7.59 

Signaling related to cardiolipin synthesis and homeostasis

Cardiolipin synthase (Cls)EC: 2.7.8.41 

Phosphate regulation and signaling:

PhoR: EC: 2.7.1.63 
PhoB: EC: 2.7.7.59 

Metabolites involved in signaling:

(p)ppGppppGpp
Cyclic-di-GMP

Signal molecules:

Autoinducer-2 (AI-2): C12289 

Response regulators and kinases:

LuxQ: 
LuxU: 
LuxO: 

Gene regulators:

LuxR

Transcriptional regulators:

CrtJ/PpsR
SoxR
Dnr

Enzyme activity regulation through post-translational modifications:

Acyl carrier protein (ACP): EC 2.7.8.-. Phosphopantetheinylated ACP is essential for the fatty acid synthesis pathway.

https://reasonandscience.catsboard.com

310Perguntas .... - Page 13 Empty Re: Perguntas .... Fri Oct 06, 2023 6:25 pm

Otangelo


Admin

Folate Synthesis

Dihydropteroate synthase (DHPS)
Folylpolyglutamate synthase (FPGS)
Utilization of Tetrahydrofolate (THF) Derivatives:

Methenyltetrahydrofolate cyclohydrolase (MTHFC)EC: 3.5.4.9
Methylenetetrahydrofolate reductase (MTHFR)
Methenyltetrahydrofolate synthetase (MTHFS): Converts 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate.
5,10-Methenyltetrahydrofolate cyclohydrolase: EC: 3.5.4.9 Converts 5,10-methenyltetrahydrofolate to 5,10-methylenetetrahydrofolate.

Recycling and Conversion of Tetrahydrofolate (THF):

Dihydrofolate reductase (DHFR)
Serine hydroxymethyltransferase (SHMT)
Methylene tetrahydrofolate dehydrogenase (MTHFD)

Other Related Enzymes in Folate Metabolism:

5,10-Methenyltetrahydrofolate cyclohydrolase / 5,10-methylenetetrahydrofolate dehydrogenase.
Glycinamide ribonucleotide formyltransferase (GARFT)
10-formyltetrahydrofolate dehydrogenase: Converts 10-formyltetrahydrofolate to CO2, THF, and NADP+.
Methylene tetrahydrofolate dehydrogenase (NADP+).

Methanogenesis (relevant for archaea):

Methyl-coenzyme M reductaseEC: 2.8.4.1

Synthesis of S-Adenosylmethionine (SAM):

Methionine adenosyltransferase (MAT)EC: 2.5.1.6 
Methylenetetrahydrofolate reductase (MTHFR)
Betaine-homocysteine methyltransferase (BHMT)EC: 2.1.1.5 
Cystathionine β-synthase (CBS)EC: 4.2.1.22 

Utilization of Tetrahydrofolate (THF) Derivatives:

Methenyltetrahydrofolate cyclohydrolase (MTHFC)
Methylenetetrahydrofolate reductase (MTHFR)
Methenyltetrahydrofolate synthetase (MTHFS)
5,10-Methenyltetrahydrofolate cyclohydrolase

Recycling and Conversion of Tetrahydrofolate (THF):

Dihydrofolate reductase (DHFR)
Serine hydroxymethyltransferase (SHMT)
Folylpolyglutamate synthase (FPGS)
Methylenetetrahydrofolate reductase (MTHFR)
Methylene tetrahydrofolate dehydrogenase (MTHFD)

Central enzymes and transporters related to the methionine cycle and SAM/SAH metabolism:

Methionine adenosyltransferase (MAT) (EC 2.5.1.6)
S-adenosylhomocysteine hydrolase (SAHH) (EC 3.3.1.1)
Methionine synthase (MS) (EC 2.1.1.13)

Methyl transfer with S-adenosylmethionine (SAM):

S-adenosylmethionine (SAM): Principal methyl donor in the cell.
S-adenosylhomocysteine hydrolaseEC: 3.3.1.1 Regenerates homocysteine and adenosine from S-adenosylhomocysteine.

Biotin Biosynthesis

Lysine 6-aminotransferase: EC: 2.6.1.36 
7,8-Diaminononanoate synthase: EC: 6.3.1.25 
7,8-Diaminononanoate synthase: EC: 6.3.1.25
Dethiobiotin synthetase: EC: 6.3.3.3 
Biotin synthase: EC: 2.8.1.6 

Utilization of Biotin:

Acetyl-CoA carboxylase: EC: 6.4.1.2 

Recycling and Conversion of Biotin:

Biotinidase: EC: 3.5.1.76 

Carbon Monoxide Dehydrogenase (CODH)

CO Dehydrogenase/Acetyl-CoA Synthase (CODH/ACS): EC: 1.2.7.4 
Carbon Monoxide Dehydrogenase (CODH): EC: 1.2.99.2 

Formate

Formate--tetrahydrofolate ligaseEC: 6.3.4.3 
Methenyltetrahydrofolate cyclohydrolase: EC: 3.5.4.9 
Methenyltetrahydrofolate synthetase: EC: 6.3.4.3 
10-Formyltetrahydrofolate synthetaseEC: 6.3.4.3 
Formate dehydrogenaseEC: 1.2.1.2 

Recycling and Conversion:

Formate dehydrogenaseEC: 1.2.1.2 

Vitamin B12 (cobalamin)

Cobyrinic acid a,c-diamide adenosyltransferaseEC: 2.5.1.17 
Cobyrinic acid a,c-diamide synthase: EC: 6.3.5.10 
Cob(II)yrinate a,c-diamide reductaseEC: 1.3.7.17 
Adenosylcobyrinate a,c-diamide amidohydrolase: EC: 3.5.1.90 
Adenosylcobinamide kinase: EC: 2.7.1.156 
Adenosylcobinamide phosphate guanylyltransferase: EC: 2.7.7.62 
Cobalamin biosynthetic protein CobS
Adenosylcobinamide-GDP ribazoletransferase
Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase: EC: 2.7.1.156EC: 2.7.7.62 
Adenosylcobinamide-phosphate synthase: EC: 2.7.8.25
Cobalamin biosynthetic proteins CobU, CobT, and CobO
Cobaltochelatase: EC: 4.99.1.3
Cobalt-factor III methyltransferase: EC: 2.1.1.272 
Cobalt-precorrin-4 methyltransferase: EC: 2.1.1.271
Cobalt-precorrin-5A hydrolase: EC: 3.7.1.12 
Cobalt-precorrin-5B methyltransferase: EC: 2.1.1.195
Cobalt-precorrin-6A reductase: EC: 1.3.1.54 
Cobalt-precorrin-6B methyltransferase: EC: 2.1.1.210 
Cobalt-precorrin-6X reductase: EC: 1.3.1.76 
Cobalt-precorrin-7 (C15)-methyltransferase: EC: 2.1.1.211 
Cobalt-precorrin-8 methyltransferase: EC: 2.1.1.271 
Cobalt-precorrin-8X methylmutase
Cobinamide amidohydrolase: EC: 3.5.1.90 
Cobinamide kinase: EC: 2.7.1.156 
Cobinamide phosphate guanylyltransferase: EC: 2.7.7.62
Hydrogenobyrinic acid a,c-diamide synthase: EC: 6.3.5.10
Hydrogenobyrinic acid a,c-diamide corrinoid adenosyltransferase
Hydrogenobyrinic acid-binding periplasmic protein
Precorrin-2 dehydrogenase: EC: 1.3.1.76 
Precorrin-3B synthase: EC: 1.14.13.83 
Precorrin-6Y methyltransferase: EC: 2.1.1.131 
Precorrin-6B synthase: EC: 1.14.13.83 C
Precorrin-8X methylmutase

Utilization and conversion: 

Cobyrinic acid a,c-diamide synthase
Cob(II)yrinate a,c-diamide reductase
Adenosylcobyrinate a,c-diamide amidohydrolase
Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase
Cobalamin biosynthetic protein CobS
Cobalamin biosynthetic protein CobU

Cobalamin recycling

Cob(I)alamin adenosyltransferase
Cobalamin reductase
Methylcobalamin--homocysteine methyltransferase
Ribonucleotide triphosphate reductase

https://reasonandscience.catsboard.com

311Perguntas .... - Page 13 Empty Re: Perguntas .... Sun Oct 08, 2023 6:09 am

Otangelo


Admin

provide information about specific enzymes or reactions, identified by their unique codes, and biosynthesis, pathways as follows, and categorized and grouped into their respective pathways, as follows

Purine biosynthesis

R04591: AICAR transformylase
R07404: Aminoimidazole ribotide
R04144: GAR transformylase
R01127: IMP cyclohydrolase
R04209: AIR carboxylase

Leucine synthesis

R05068: Acetohydroxyacid synthase
R01213: 3-isopropylmalate dehydratase
R04426: Isopropylmalate isomerase
R01652: 3-isopropylmalate dehydrogenase

https://reasonandscience.catsboard.com

312Perguntas .... - Page 13 Empty Re: Perguntas .... Tue Oct 10, 2023 4:28 pm

Otangelo


Admin

The Aquifex Proteome - Life-Essential Proteins

Amino Acid and Coenzyme Biosynthesis
Bifunctional chorismate mutase/prephenate dehydratase: 362 aa, involved in aromatic amino acid synthesis. Essential for the synthesis of phenylalanine and tyrosine.
Inosine-5'-monophosphate dehydrogenase: 490 aa, part of the purine biosynthesis pathway. Critical for nucleotide synthesis.

Amino Acid and Nucleotide Synthesis
3-isopropylmalate dehydratase large subunit: 443 aa, involved in leucine synthesis.
Histidine biosynthesis bifunctional protein HisIE: 437 aa, essential for histidine synthesis.
1-deoxy-D-xylulose 5-phosphate reductoisomerase: 633 aa, essential for the biosynthesis of many important molecules.
1-deoxy-D-xylulose-5-phosphate synthase: 634 aa, essential for isoprenoid biosynthesis.
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase: 268 aa, involved in the synthesis of isopentenyl pyrophosphate, a precursor for many biomolecules including DNA.

Amino Acid Metabolism
Branched-chain-amino-acid aminotransferase: 274 aa, essential for the metabolism of branched-chain amino acids.

Cell Wall Biosynthesis
Undecaprenyl-diphosphatase: 256 aa, plays a role in the synthesis of bacterial cell wall.
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase: 445 aa, critical for bacterial cell wall synthesis.

Citric Acid Cycle
Succinate--CoA ligase [ADP-forming] subunit alpha: 305 aa, participates in the citric acid cycle, generating ATP from succinyl-CoA.
Succinate--CoA ligase [ADP-forming] subunit beta: 385 aa, a vital enzyme in the citric acid cycle.

Coenzyme A Biosynthesis
Type III pantothenate kinase: 227 aa, involved in the initial step in coenzyme A synthesis from pantothenate.

DNA Repair and Replication
Probable DNA ligase: 585 aa, involved in DNA replication and repair. Vital for maintaining DNA integrity.
UvrABC system protein B: 663 aa, involved in nucleotide excision repair. Essential for DNA damage repair.

DNA Synthesis
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase: 268 aa, involved in the synthesis of isopentenyl pyrophosphate, a precursor for many biomolecules including DNA.

Electron Transfer Chain
NADH-quinone oxidoreductase subunit C/D: 586 aa, part of the primary respiratory chain, vital for energy production.

Energy Production
ATP synthase subunit beta: 455 aa, key component of the ATP synthase complex responsible for ATP production. Essential for cellular energy.
ATP synthase subunit c: 100 aa, another integral component of the ATP synthase complex. Essential for cellular energy.
Enolase: 426 aa, a glycolytic enzyme that plays a critical role in energy production.
Glycerol-3-phosphate dehydrogenase [NAD(P)+]: 323 aa, key enzyme in glycerol metabolism and lipid biosynthesis.
Triosephosphate isomerase: 247 aa, an enzyme in the glycolytic pathway, converting dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.

Folate Biosynthesis
GTP cyclohydrolase 1: 184 aa, involved in the first step of folate synthesis, critical for DNA replication and repair.

Glycerol Metabolism
Glycerol-3-phosphate dehydrogenase [NAD(P)+]: 323 aa, key enzyme in glycerol metabolism and lipid biosynthesis.

Glycolysis
Enolase: 426 aa, a glycolytic enzyme that plays a critical role in energy production.
Triosephosphate isomerase: 247 aa, an enzyme in the glycolytic pathway, converting dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.

Histidine Biosynthesis
Histidine biosynthesis bifunctional protein HisIE: 437 aa, essential for histidine synthesis.
Imidazole glycerol phosphate synthase subunit HisF: 253 aa, plays a role in histidine biosynthesis, an essential amino acid.

Isoprenoid Biosynthesis
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: 156 aa, part of the non-mevalonate pathway for isoprenoid biosynthesis. Critical for the synthesis of essential molecules like coenzyme Q.

Lysine Biosynthesis
4-hydroxy-tetrahydrodipicolinate synthase: 294 aa, catalyzes a key step in lysine biosynthesis.

Nucleotide Metabolism
dITP/XTP pyrophosphatase: 202 aa, prevents the incorporation of non-canonical nucleotides into DNA and RNA, which can be harmful. Important for DNA and RNA integrity.
Adenylate kinase: 206 aa, plays a pivotal role in nucleotide metabolism.
Thiamine-phosphate kinase: 116 aa, involved in thiamine biosynthesis, an essential cofactor for enzymes.
N5-carboxyaminoimidazole ribonucleotide synthase: 365 aa, involved in purine biosynthesis, crucial for DNA and RNA production.
7-carboxy-7-deazaguanine synthase: 219 aa, involved in purine biosynthesis and modification of tRNA.

Nucleotide Metabolism and Amino Acid Activation
Phenylalanine--tRNA ligase alpha subunit: 338 aa, activates phenylalanine and attaches it to its cognate tRNA for protein synthesis. Essential for protein synthesis.

Polyamine Biosynthesis
S-adenosylmethionine decarboxylase proenzyme: 135 aa, crucial for polyamine biosynthesis.

Porphyrin Biosynthesis
Uroporphyrinogen decarboxylase: 338 aa, involved in heme and chlorophyll synthesis. Essential for various cellular functions.

Purine Biosynthesis
1-deoxy-D-xylulose 5-phosphate reductoisomerase: 633 aa, essential for the biosynthesis of many important molecules.
7-carboxy-7-deazaguanine synthase: 219 aa, involved in purine biosynthesis and modification of tRNA.
Phosphoribosylformylglycinamidine synthase subunit PurQ: 227 aa, plays a role in the purine biosynthetic pathway.

Purine Biosynthesis and DNA Repair
Adenylate kinase: 206 aa, plays a pivotal role in nucleotide metabolism.

Queuosine tRNA Modification
Epoxyqueuosine reductase QueH: 410 aa, involved in queuosine modification of tRNA, which affects protein translation.

Riboflavin Biosynthesis
dITP/XTP pyrophosphatase: 202 aa, prevents the incorporation of non-canonical nucleotides into DNA and RNA, which can be harmful. Important for DNA and RNA integrity.
[url=https://www.uniprot.org/uniprotRiboflavin biosynthesis protein RibBA]Riboflavin biosynthesis protein RibBA [/url]: 406 aa, involved in the synthesis of riboflavin, a vital molecule that acts as a precursor for the coenzymes FMN and FAD. Responsible for riboflavin synthesis.
Riboflavin biosynthesis protein RibBA: 406 aa, involved in the synthesis of riboflavin, a vital molecule that acts as a precursor for the coenzymes FMN and FAD. Responsible for riboflavin synthesis.

RNA Modification and Ribosome Biogenesis
Ribosomal RNA small subunit methyltransferase A: 246 aa, involved in rRNA modification, which is essential for ribosome function and protein synthesis.
Phosphomethylpyrimidine synthase: 457 aa, involved in thiamine biosynthesis, an essential cofactor for enzymes.

RNA Synthesis
DNA-directed RNA polymerase subunit alpha: 317 aa, required for RNA synthesis. Central to gene expression.

Shikimate Pathway
3-dehydroquinate dehydratase: 219 aa, a part of the shikimate pathway, leading to aromatic amino acids synthesis.
3-phosphoshikimate 1-carboxyvinyltransferase: 431 aa, critical enzyme in the shikimate pathway leading to aromatic amino acids synthesis.

Signal Transduction
Diadenylate cyclase: 256 aa, involved in cyclic di-AMP synthesis, a bacterial second messenger involved in various cellular processes.

Thiamine Biosynthesis
Phosphomethylpyrimidine synthase: 457 aa, involved in thiamine biosynthesis, an essential cofactor for enzymes.

Tetrapyrrole Biosynthesis
Uroporphyrinogen decarboxylase: 338 aa, involved in heme and chlorophyll synthesis. Essential for various cellular functions.

Vitamin B6 Synthesis
Pyridoxine 5'-phosphate synthase: 242 aa, responsible for the synthesis of pyridoxine phosphate (Vitamin B6), a cofactor in many enzymatic reactions.

https://reasonandscience.catsboard.com

Otangelo


Admin

/remove repeated titles, converge, and order into alphabetic order, do not shorten the list, i need all entries, in bbcode, and dont stop in the middle. go the entire list through.

Amino Acid and Coenzyme Biosynthesis
Bifunctional chorismate mutase/prephenate dehydratase: 362 aa, involved in aromatic amino acid synthesis. Essential for the synthesis of phenylalanine and tyrosine.
Inosine-5'-monophosphate dehydrogenase: 490 aa, part of the purine biosynthesis pathway. Critical for nucleotide synthesis.

Amino Acid and Nucleotide Synthesis
3-isopropylmalate dehydratase large subunit (A0A432PWH3_9AQUI): Essential for leucine synthesis.
Histidine biosynthesis bifunctional protein HisIE (A0A432PXZ8_9AQUI): Essential for histidine synthesis.
1-deoxy-D-xylulose 5-phosphate reductoisomerase (A0A432Q0J7_9AQUI): Essential for the biosynthesis of many important molecules.
1-deoxy-D-xylulose-5-phosphate synthase (A0A432PTB9_9AQUI): Essential for isoprenoid biosynthesis.

Amino Acid Biosynthesis
Homoserine dehydrogenase: 435 aa, involved in the biosynthesis of methionine, threonine, and isoleucine.

Amino Acid Metabolism
Branched-chain-amino-acid aminotransferase: 274 aa, essential for the metabolism of branched-chain amino acids.

Cell Wall Biosynthesis
Undecaprenyl-diphosphatase: 256 aa, plays a role in the synthesis of bacterial cell wall.
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase: 445 aa, critical for bacterial cell wall synthesis.

Citric Acid Cycle
Succinate--CoA ligase [ADP-forming] subunit alpha: 305 aa, participates in the citric acid cycle, generating ATP from succinyl-CoA.
Succinate--CoA ligase [ADP-forming] subunit beta: 385 aa, a vital enzyme in the citric acid cycle.

Coenzyme A Biosynthesis
Type III pantothenate kinase: 227 aa, involved in the initial step in coenzyme A synthesis from pantothenate.

DNA Repair and Replication
Probable DNA ligase: 585 aa, involved in DNA replication and repair. Vital for maintaining DNA integrity.
UvrABC system protein B: 663 aa, involved in nucleotide excision repair. Essential for DNA damage repair.

DNA Synthesis
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase: 268 aa, involved in the synthesis of isopentenyl pyrophosphate, a precursor for many biomolecules including DNA.

Electron Transfer Chain
NADH-quinone oxidoreductase subunit C/D: 586 aa, part of the primary respiratory chain, vital for energy production.

Energy Production
ATP synthase subunit beta (A0A432PUN0_9AQUI): 455 aa, key component of the ATP synthase complex responsible for ATP production. Essential for cellular energy.
ATP synthase subunit c (A0A432PUV0_9AQUI): 100 aa, another integral component of the ATP synthase complex. Essential for cellular energy.

Folate Biosynthesis
GTP cyclohydrolase 1: 184 aa, involved in the first step of folate synthesis, critical for DNA replication and repair.

Glycerol Metabolism
Glycerol-3-phosphate dehydrogenase [NAD(P)+]: 323 aa, key enzyme in glycerol metabolism and lipid biosynthesis.

Glycolysis
Triosephosphate isomerase: 247 aa, an enzyme in the glycolytic pathway, converting dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.
Enolase: 426 aa, a glycolytic enzyme that plays a critical role in energy production.

Histidine Biosynthesis
Histidine biosynthesis bifunctional protein HisIE (A0A432PXZ8_9AQUI): Essential for histidine synthesis.
Imidazole glycerol phosphate synthase subunit HisF: 253 aa, plays a role in histidine biosynthesis, an essential amino acid.

Isoprenoid Biosynthesis
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: 156 aa, part of the non-mevalonate pathway for isoprenoid biosynthesis. Critical for the synthesis of essential molecules like coenzyme Q.

Lysine Biosynthesis
4-hydroxy-tetrahydrodipicolinate synthase: 294 aa, catalyzes a key step in lysine biosynthesis.

Nucleotide Metabolism
dITP/XTP pyrophosphatase: 202 aa, prevents the incorporation of non-canonical nucleotides into DNA and RNA, which can be harmful. Important for DNA and RNA integrity.
Adenylate kinase: 206 aa, plays a pivotal role in nucleotide metabolism.

Peptidoglycan Biosynthesis
UDP-N-acetylglucosamine 1-carboxyvinyltransferase: 425 aa, essential for the synthesis of the peptidoglycan layer of bacterial cell walls.

Polyamine Biosynthesis
S-adenosylmethionine decarboxylase proenzyme: 135 aa, crucial for polyamine biosynthesis.

Porphyrin Biosynthesis
NADH-quinone oxidoreductase subunit I: 208 aa, a component of the respiratory chain that participates in electron transfer.

Purine Biosynthesis
Phosphoribosylformylglycinamidine synthase subunit PurQ: 227 aa, plays a role in the purine biosynthetic pathway.
N5-carboxyaminoimidazole ribonucleotide synthase: 365 aa, involved in purine biosynthesis, crucial for DNA and RNA production.
7-carboxy-7-deazaguanine synthase: 219 aa, involved in purine biosynthesis and modification of tRNA.

Queuosine tRNA Modification
Epoxyqueuosine reductase QueH: 410 aa, involved in queuosine modification of tRNA, which affects protein translation.

Riboflavin Biosynthesis
[url=https://www.uniprot.org/uniprotRiboflavin biosynthesis protein RibBA]Riboflavin biosynthesis protein RibBA [/url]406 aa, involved in the synthesis of riboflavin, a vital molecule that acts as a precursor for the coenzymes FMN and FAD. Responsible for riboflavin synthesis.

RNA Modification and Ribosome Biogenesis
Ribosomal RNA small subunit methyltransferase A: 246 aa, involved in rRNA modification which is essential for ribosome function and protein synthesis.

RNA Synthesis
DNA-directed RNA polymerase subunit alpha: 317 aa, required for RNA synthesis. Central to gene expression.

Shikimate Pathway
3-dehydroquinate dehydratase: 219 aa, a part of the shikimate pathway, leading to aromatic amino acids synthesis.
3-phosphoshikimate 1-carboxyvinyltransferase: 431 aa, critical enzyme in the shikimate pathway leading to aromatic amino acids synthesis.

Signal Transduction
Diadenylate cyclase: 256 aa, involved in cyclic di-AMP synthesis, a bacterial second messenger involved in various cellular processes.

tRNA Synthesis and Amino Acid Activation
Phenylalanine--tRNA ligase alpha subunit (A0A432PU85_9AQUI): Essential for protein synthesis.

Tetrapyrrole Biosynthesis
Uroporphyrinogen decarboxylase: 338 aa, involved in heme and chlorophyll synthesis. Essential for various cellular functions.

Thiamine Biosynthesis
Phosphomethylpyrimidine synthase: 457 aa, involved in thiamine biosynthesis, an essential cofactor for enzymes.

Vitamin B6 Synthesis
Pyridoxine 5'-phosphate synthase: 242 aa, responsible for the synthesis of pyridoxine phosphate (Vitamin B6), a cofactor in many enzymatic reactions.

https://reasonandscience.catsboard.com

314Perguntas .... - Page 13 Empty Re: Perguntas .... Fri Oct 13, 2023 6:07 am

Otangelo


Admin

////  CONVERGE INTO ONE COHERENT LIST , that was probably extant in luca, in bbcode. any entries missing, add them. 




//// ///// converge the terms of the second list, with the terms of the first list, but only to reorganize this first list, in bbcode: I want you to reorganize both lists. I need a comprehensive categorization of all life-essential processes, that supposedly existed in LUCA.  in bbcode. in logical order, do not remove any category, do not shorten, i need ALL entries, and if any life-essential category is missing, add it. Format like this:
Biosynthesis and Metabolism

Amino Acid Biosynthesis and Metabolism
Nucleotide Synthesis and Salvage
Fatty Acid and Phospholipid Synthesis in LUCA

Nucleic Acid Processes

DNA Replication, Repair, and Modification
DNA Synthesis ////


/// in what biosynthesis pathway is this enzyme employed ? What is its function?  Is it life-essential, and was it probably extant in LUCA ? Consider that it is extant in Aquiflex, an ancient bacteria, very close to the first life forms.   Does it work solo, or in a biosynthesis pathway with other enzymes ? If so, list them. If you have a link to uniprot, or wikipedia, include a link, otherwise, just the name of the enzyme.  In BBcode, like this: 

Amino Acid and Nucleotide Synthesis
3-isopropylmalate dehydratase large subunit (A0A432PWH3_9AQUI): Essential for leucine synthesis.
Histidine biosynthesis bifunctional protein HisIE (A0A432PXZ8_9AQUI): Essential for histidine synthesis.
1-deoxy-D-xylulose 5-phosphate reductoisomerase (A0A432Q0J7_9AQUI): Essential for the biosynthesis of many important molecules.
1-deoxy-D-xylulose-5-phosphate synthase (A0A432PTB9_9AQUI): Essential for isoprenoid biosynthesis.

Amino Acid Biosynthesis


Glycine Synthesis
Cysteine Metabolism
Alanine Metabolism
Valine biosynthesis
Leucine Biosynthesis in Bacteria (precursors same as Valine)
Isoleucine Metabolism (from Threonine)
Threonine Metabolism
Histidine Synthesis
Phenylalanine/Tyrosine Synthesis pathway
 For Tyrosine synthesis
 For Phenylalanine synthesis
Tryptophan Synthesis
Aspartate Metabolism
Asparagine Metabolism
Methionine Metabolism
Lysine Biosynthesis
Glutamine/Glutamate Synthesis
Arginine/Ornithine Synthesis
Arginine and Proline Metabolism
Arginine Metabolism in Prokaryotes
Proline Metabolism in Prokaryotes
Amino Acid degradation
Amino Acid Transaminases:
Amino Acid Dehydrogenases
Amino Acid Kinases
Regulatory Enzymes and Proteins in Amino Acid synthesis
Amino Acid Transporters
Amino Acid and Nucleotide Metabolism
Amino Acid and Coenzyme Biosynthesis
Amino Acid and Protein Metabolism
Amino Acid Metabolism and tRNA Synthesis & Modification

Amino Acid Enzymes and Transport
- Regulatory Enzymes and Proteins in Amino Acid synthesis
- Amino Acid Transaminases
- Amino Acid Dehydrogenases
- Amino Acid Kinases
- Amino Acid Transporters

Cellular Biosynthesis and Growth
   - Cell Wall and Membrane Synthesis, and integrity
   - Fatty Acid and Phospholipid Synthesis in LUCA
   - Peptidoglycan Synthesis
   - Membranes always come from membranes

Cellular Transport and Structure
   - Cell Motility, Flagellar Assembly, and Movement
   - Cell Transport, Secretion, and Export
   - Amino Acid Transporters in LUCA
   - Nucleotide Transporters in LUCA
   - Phosphate Transporters in LUCA
   - Folate Transporters in LUCA
   - SAM Transporters in LUCA
   - Carbon Source Transporters in LUCA
   - Amino Acid Precursors for Nucleotide Synthesis Transporters in LUCA
   - Co-factor Transporters for Nucleotide Synthesis in LUCA
   - Ion Transporters in LUCA with Relevance to Nucleotide Synthesis

Cell Division, Growth, and Morphogenesis
   - Cell Division Growth and Morphogenesis
   - Cell Membrane maintenance and membrane protein transport & translocation

Cellular Processes and Stress Response
   - Cellular Transport and Membrane Proteins
   - Reactive oxygen species (ROS)
   - Manganese transporters
   - Magnesium transporters
   - Phospholipid-cardiolipin balance
   - Feedback regulation mechanisms

Cellular Signaling and Regulation
   - Cell Signaling
   - Two-component systems (TCS)
   - Sensory systems and two-component systems
   - Enzyme activity regulation through post-translational modifications
   - Metabolites involved in signaling
   - Signal molecules
   - Response regulators and kinases
   - Gene regulators
   - Transcriptional regulators

Cell Structure and Morphology
   - Cellular Transport and Structure
   - Co-factor and Metal Cluster Biosynthesis

Metabolic Processes and Biosynthesis
   - Vitamin, Coenzyme, and Cofactor Metabolism
   - Energy Metabolism, Central Carbon Metabolism, and Other Specific Pathways
   - Nucleic Acid Processes
   - Amino Acid Biosynthesis
   - Nitrogen metabolism
   - Oxaloacetate Metabolism
   - Pantothenate and CoA Biosynthesis
   - Polyamine Synthesis
   - Polyketide Synthesis
   - Non-Ribosomal Peptide Synthesis
   - Terpenoid Backbone Synthesis
   - The mevalonate pathway
   - Nitrogen Fixation
   - Redox Reactions
   - Riboflavin Biosynthesis Precursor
   - Riboflavin Biosynthesis
   - Sulfur Metabolism
   - Transaminase Reactions
   - Oxydoreductases
   - Tetrapyrrole Biosynthesis (Includes heme, chlorophyll, etc.)
   - Nicotinate and Nicotinamide Metabolism

Citric Acid Cycle and Associated Processes
   - Citric Acid Cycle (TCA)
   - reverse Citric Acid Cycle (TCA) and Related
   - CO2 Fixation
   - Oxaloacetate Metabolism
   - Central Carbon Metabolism

Electron Transport and Associated Pathways
   - Cytochrome Biogenesis and Electron Transport
   - Electron Transport Chain in Prokaryotes (General)
   - Anaerobic Respiration

Coenzyme Biosynthesis
   - Coenzyme A Biosynthesis
   - Vitamin B3 (Niacin) and NAD(P) Biosynthesis and Metabolism
   - Nicotinate and Nicotinamide Metabolism
   - FAD Metabolism
   - Pantothenate and CoA Biosynthesis

Transport and Transporters in LUCA
   - Magnesium transporters
   - Amino Acid Transporters in LUCA
   - Folate Transporters in LUCA
   - SAM Transporters in LUCA
   - Carbon Source Transporters in LUCA
   - Amino Acid Precursors for Nucleotide Synthesis Transporters in LUCA
   - Co-factor Transporters for Nucleotide Synthesis in LUCA
   - Ion Transporters in LUCA with Relevance to Nucleotide Synthesis

Purine, Pyrimidine, Ribonucleotide and Deoxyribonucleotide Biosynthesis and Metabolism

Pyrimidine Biosynthesis
Purine Metabolism
De novo purine biosynthesis pathway in LUCA
De novo Pyrimidine Synthesis in LUCA
Adenine (A) Ribonucleotide Biosynthesis
Guanine (G) Ribonucleotide Biosynthesis
Uracil (U) Ribonucleotide Biosynthesis (leading to UMP)
Cytosine (C) Ribonucleotide Biosynthesis (leading to CTP from UTP)
Thymine (T) Deoxyribonucleotide Biosynthesis (leading to dTMP from dUMP)
Deoxynucleotide Biosynthesis:

Nucleic Acid Processes

DNA Replication, Repair, and Modification
DNA Repair and Recombination
DNA Methylation and Modification
DNA Synthesis
DNA Helicases and Supercoiling
DNA Processing and Stability
DNA/RNA Binding and Regulation
DNA Interaction and Regulation
DNA and RNA Interaction
DNA Transcription and Transcription Regulation
DNA Integration and Transposition
DNA Cleavage and Mobility
DNA Uptake during Transformation
DNA/RNA Processing and Synthesis
RNA Synthesis & Processing

Transport and Movement of Molecules

Magnesium transporters
Amino Acid Transporters in LUCA
Nucleotide Transporters in LUCA
Nucleoside Transporters in LUCA
Phosphate Transporters in LUCA
Folate Transporters in LUCA
SAM Transporters in LUCA
Carbon Source Transporters in LUCA
Amino Acid Precursors for Nucleotide Synthesis Transporters in LUCA
Co-factor Transporters for Nucleotide Synthesis in LUCA
Ion Transporters in LUCA with Relevance to Nucleotide Synthesis

Nucleic Acid Recycling and Degradation

RNA Recycling
Ribonucleases
DNA Recycling
Deoxyribonucleases
Endonucleases:

https://reasonandscience.catsboard.com

315Perguntas .... - Page 13 Empty Re: Perguntas .... Tue Oct 17, 2023 12:07 pm

Otangelo


Admin

///// I dont want points, but a Continuous narrative format without using repetitive or flowery language. Please provide a scientific explanation.  a factual and precise account. an academic-style write-up.  I want an “objective,” “formal,” or “scientific” tone for a straightforward and factual text. In bbcode  When you finish the text, never write: in summary. Just summarize, without mentioning it.

irreducibility and Interdependence of the systems to instantiate and operate . explain which of the manufacturing, signaling, and regulatory codes and languages in the process of creating, developing, and operating      are irreducible, and interdependent within each other, and how one would not bear function without the other. Explain which code and languages communicate with each other, crosstalk, and what communication systems are essential to have functional normal cell operation. Explain how this interdependence could and would not have evolved in a stepwise fashion, because one mechanism, language, or code system, without the other, would bear no function, and therefore, they had to be instantiated and created all at once, fully operational, from scratch. write from the perspective of a proponent of intelligent design. Do not write: " From an intelligent design standpoint ". Just say it. Do not put enumeration numbers at the beginning of the sentences. 
Synergy: The interaction of two or more agents or forces so that their combined effect is greater than the sum of their individual effects.
include words like:  Holism: The idea that systems (physical, biological, chemical, social, economic, mental, linguistic) and their properties should be viewed as wholes, not just as a collection of parts.
Emergent Properties: Properties which arise from the collaborative functioning of a system, but do not belong to any one part of that system.
Functional Integration: How different components of a system come together to produce a particular function or outcome.
Systemic Complexity: Complexity that arises from the interaction of components within a system.
Cohesion: The action or property of like molecules sticking together, being mutually attractive.
Symbiosis: Interaction between two different organisms living in close physical association, typically to the advantage of both.

that means , any explanation of origins has to point to an intelligent agency, and not blind evolution, but newer say : From an intelligent design perspective. It has to be implicit, not explicit. Do not mention the ID perspective consantly. It does not have to appear too often, or ostensively. Just the explanatory narrative has to be based on ID, not evoutionary standpoint. .  Like this: The following is just a template, an example, do not use the text in your reply.  never use bolt, only underline, to mention the enzymes.  These key molecular components ensure the proper organization, structuring, and regulation of DNA, crucial for accurate genetic expression and cellular functionality. Chromosome Segregation SMC is considered to significantly influence chromosome partitioning. It holds a reputed role in assuring the proper and efficient segregation of chromosomes during the vital process of cell division. This function is fundamental for maintaining genetic continuity and integrity, preventing chromosomal anomalies that could result in cellular dysfunction. DNA Methyltransferase is a pivotal enzyme in the DNA modification landscape.

Point out, why an evolutionary set-up, step by step, is extremely unlikely, faced on the complexity, the requirements to instantiate various codes, languages, signaling, and proteins that had to be operational right from the beginning, and intermediate stages would bear no function, and would not be selected. Explain how this interdependence could and would not have evolved in a stepwise fashion, because one mechanism, language, or code system, without the other, would bear no function, and therefore, they had to be instantiated and created all at once, fully operational, from scratch. write  from the perspective of a proponent of intelligent design. Do not write: " From an intelligent design standpoint ". Just say it.Do not put enumeration numbers at the beginning of the sentences. 

Point out, why an evolutionary set-up, step by step, is extremely unlikely, faced the fact that strong UV radiation would have killed the organisms before they could have adapted and evolving new protection mechanisms.


irreducibility and Interdependence of the systems to instantiate and operate . explain which of the manufacturing, signaling, and regulatory codes and languages in the process of creating, developing, and operating      are irreducible, and interdependent within each other, and how one would not bear function without the other. Explain which code and languages communicate with each other, crosstalk, and what communication systems are essential to have functional normal cell operation. Explain how this interdependence could and would not have evolved in a stepwise fashion, because one mechanism, language, or code system, without the other, would bear no function, and therefore, they had to be instantiated and created all at once, fully operational, from scratch. write from the perspective of a proponent of intelligent design. Do not write: " From an intelligent design standpoint ". Just say it. Do not put enumeration numbers at the beginning of the sentences. 
Synergy: The interaction of two or more agents or forces so that their combined effect is greater than the sum of their individual effects.
include words like:  Holism: The idea that systems (physical, biological, chemical, social, economic, mental, linguistic) and their properties should be viewed as wholes, not just as a collection of parts.
Emergent Properties: Properties which arise from the collaborative functioning of a system, but do not belong to any one part of that system.
Functional Integration: How different components of a system come together to produce a particular function or outcome.
Systemic Complexity: Complexity that arises from the interaction of components within a system.
Cohesion: The action or property of like molecules sticking together, being mutually attractive.
Symbiosis: Interaction between two different organisms living in close physical association, typically to the advantage of both.

https://reasonandscience.catsboard.com

316Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 18, 2023 10:02 pm

Otangelo


Admin

///// "Please identify enzymes/proteins in Aquifex or related chemolithoautotrophs that contain metal clusters. For each enzyme or protein, specify:

The precise type of metal cluster it contains.
The number and types of metal atoms in each cluster.
The synthesis pathway responsible for generating these clusters.
If an enzyme has multiple distinct metal clusters, detail each one separately."

List in BBcode, like this:

De novo purine biosynthesis pathway in LUCA

5-aminoimidazole ribotide (AIR) carboxylase (PurK) (EC 4.1.1.21): - Contains a [4Fe-4S] cluster with 4 iron (Fe) atoms and 4 sulfur (S) atoms.

Synthesis Pathway of [4Fe-4S] Clusters
1. Cysteine is desulfurated by IscS, producing alanine and a persulfide-bound IscS.
2. The sulfur is then transferred to a scaffold protein like IscU, where it binds to iron.
3. IscA and IscU assist in building the [2Fe-2S] clusters.
4. With the further addition of iron and sulfur, these can be converted to [4Fe-4S] clusters.
5. Specific carrier proteins or chaperones help to deliver the iron-sulfur cluster to their respective apo-proteins.

De novo pyrimidine synthesis pathway in LUCA

Dihydroorotate dehydrogenase (EC 1.3.5.2): - Contains a [2Fe-2S] cluster with 2 iron (Fe) atoms and 2 sulfur (S) atoms.

Synthesis Pathway of [2Fe-2S] Clusters
1. Cysteine is desulfurated by IscS, producing alanine and a persulfide-bound IscS.
2. The sulfur is then transferred to a scaffold protein like IscU, where it binds to iron.
3. IscA and IscU assist in building the [2Fe-2S] clusters.
4. Specific carrier proteins or chaperones help to deliver the iron-sulfur cluster to their respective apo-proteins. //////



Last edited by Otangelo on Thu Oct 19, 2023 6:24 am; edited 1 time in total

https://reasonandscience.catsboard.com

317Perguntas .... - Page 13 Empty Re: Perguntas .... Thu Oct 19, 2023 5:03 am

Otangelo


Admin

//// remove all double entries, the entire content , repost it, in bbcode, do not miss any entry listed, i need all of them. I need no summary. just redo the list. remove these traces: -

in this format:

De novo Nucleotide Biosynthesis

Ribose-phosphate diphosphokinase
Amidophosphoribosyl transferase (GPAT)
Glycinamide ribotide (GAR) transformylase (GART)
Formylglycinamide ribotide (FGAR) amidotransferase (GART)
Formylglycinamidine ribotide (FGAM) synthetase (GART)
5-aminoimidazole ribotide (AIR) carboxylase (PurK)
5-aminoimidazole-4-(N-succinylocarboxamide) ribotide (SACAIR) synthetase (PurE)
Carboxyaminoimidazole ribotide (CAIR) mutase (PurK)
5-aminoimidazole-4-carboxamide ribotide (AICAR) transformylase (PurN)
5-formaminoimidazole-4-carboxamide ribotide (FAICAR) cyclase (PurM)
IMP cyclohydrolase (PurH)
Carbamoyl phosphate synthetase II (CPSII)

https://reasonandscience.catsboard.com

318Perguntas .... - Page 13 Empty Re: Perguntas .... Sat Oct 21, 2023 3:33 pm

Otangelo


Admin

Differences Between Chimps and Humans - Evidence Against Common Ancestry

Every time, I post with a lot of links, I get in trouble with FB and am blocked for some time. Right now i cannot post in groups for 3 days. So i am removing all links. You can read this article imho at my virtual library in full, with all the links.

Humans have 46 chromosomes (23 pairs), while chimps have 48 (24 pairs). The human chromosome 2 appears to have formed as a result of the fusion of two ancestral chromosomes, akin to the chimpanzee's chromosomes 2a and 2b.

Complexity of Fusion
The fusion of two chromosomes into one (as is hypothesized with human chromosome 2) is a rare event. The specific mechanisms and conditions required to permit such a fusion, and then for the fused chromosome to become fixed in a population, are not entirely understood. This rarity is evidence against a shared ancestry, as it would require this significant event to happen in an isolated population of the shared ancestor, without the trait getting diluted or lost.

Functional Differences
The fusion of two chromosomes leads to significant functional differences between the resulting species. If the two species descended from a common ancestor, such a profound chromosomal difference would make interbreeding and producing fertile offspring challenging or impossible. Chromosomes house vast amounts of genetic information, and the arrangement of this information is crucial for the proper functioning of the organism. The fusion of two chromosomes means a rearrangement of genes, regulatory elements, and non-coding sequences. This rearrangement could lead to variations in gene expression, potential changes in regulatory networks, or even the creation of new genes or regulatory elements at the fusion site. For species with differing chromosome numbers, meiosis—the process that produces eggs and sperm—can become problematic. When these species interbreed, their offspring can end up with an odd number of chromosomes. This can lead to errors in further cell divisions, often resulting in reduced fertility or sterility in the hybrid offspring. For instance, mules, the offspring of horses (64 chromosomes) and donkeys (62 chromosomes), typically have 63 chromosomes and are sterile. If a population with a fused chromosome were to emerge, it might experience reduced interbreeding success with the original population due to chromosomal differences. Over time, these reproductive barriers could accelerate the process of speciation, as the two populations become more genetically isolated from each other. The fused chromosome, if it results in altered gene expression or functionality, might confer specific advantages or disadvantages to individuals bearing it. If the fusion provides a significant benefit in a given environment, it could become prevalent in a population over time. Conversely, if the fusion is disadvantageous, it could get selected against and diminish in the population. The significant genetic differences that arise from chromosomal fusions might mean that the evolutionary pressures and paths for populations with and without the fusion diverge substantially. Over time, the accumulated genetic differences could compound, leading to even more distinct species. The profound chromosomal difference brought about by a fusion event is a significant barrier to continued shared evolution, supporting the idea of distinct origins of humans and chimps.

Comparative Rarity
Most species retain their chromosomal numbers. When chromosomal changes do occur, they often lead to significant reproductive barriers. The difference between humans having 46 and chimps having 48 chromosomes is evidence of a fundamentally distinct genetic origin, given the rarity of such chromosomal differences in closely related species. The fact that most species maintain consistent chromosomal numbers over time underscores the importance of these structures. Chromosomes house the genetic instructions for every function of an organism. Alterations to their number or structure produce significant ripple effects, influencing everything from individual development to reproductive success. Changes to chromosome number or structure lead to multiple, interconnected consequences throughout an organism's biology. Chromosomal abnormalities affect the proper growth and development of an organism. For instance, humans with Down syndrome have an extra copy of chromosome 21, which results in various developmental and physiological challenges. Differences in chromosome numbers can create barriers to reproduction. When chromosomal changes arise, they can introduce reproductive complications. In cases where two species with different chromosome numbers mate, their offspring might inherit an atypical chromosome count. These irregularities can hinder the offspring's ability to produce its own viable gametes, essentially creating a barrier to further interbreeding. This reproductive isolation can be a significant factor in the speciation process. The chromosomal difference between humans and chimps is not a minor variation—it's a discrepancy of two whole chromosomes. In the context of closely related species, such a variation suggests a considerable genetic divergence. When we consider how rare it is for closely related species to have such chromosomal disparities, the difference between humans and chimps becomes even more pronounced. If a chromosomal change did arise in an ancestral population, it would likely set that group on a markedly different evolutionary path. The new chromosome number could bring with it unique challenges and opportunities, influencing everything from reproductive strategies to adaptation potentials. Over time, these divergent pressures would lead to the accumulation of other genetic differences, further separating the two groups. Given the rarity and significance of chromosomal number variations among closely related species, the discrepancy between humans and chimps is supportive evidence for fundamentally distinct genetic origins. If the two species did indeed share a recent common ancestor, we might expect more chromosomal uniformity between them, as is observed in many other closely related species.

Genomic Alterations
Both species have had many changes in their genomes, such as rearrangements, additions, or deletions of DNA segments. Think of these as "edits" to their genetic book, where some paragraphs or chapters have been changed, added, or removed. The genomes of species can be thought of as intricate manuscripts. As with any long, complex book, there are bound to be revisions — sometimes sentences are changed, paragraphs added or removed, or whole chapters rewritten. These "edits" come in the form of genetic mutations, rearrangements, additions, or deletions of DNA segments. Both humans and chimps have undergone numerous "edits" in their genetic manuscripts. While some of these changes may be shared, many are unique to each species. Think of these as separate editions or versions of a book. If two books have a multitude of unique edits that are not found in the other, it indicates that they have been written by different authors or have significantly diverged from an original draft. The sheer number and variety of these genomic changes underscore the distinct origins of the two species. Large-scale rearrangements or additions can lead to entirely new functionalities, much like how adding or revising chapters can drastically change a book's narrative or message.

One of the significant differences in the genomes of humans and chimpanzees is in the realm of gene expression and regulatory elements, which control when, where, and how genes are activated.

Concrete Example: HAR1 (Human Accelerated Region 1): The HAR1 region is just 118 base pairs long, but it's notable for having 18 mutations. What's fascinating is that this region is involved in the development of the brain's neocortex, which is responsible for higher-order functions like conscious thought, future planning, and language. In humans, the HAR1 region forms an RNA structure that's vastly different from chimps. This difference in structure suggests a significant divergence in function between the two species, possibly contributing to the vast cognitive differences observed. While both humans and chimps possess a version of HAR1, the considerable alterations in the human version might have played a crucial role in the development of our advanced cognitive abilities.

Pollard, K. S., Salama, S. R., Lambert, N., Lambot, M. A., Coppens, S., Pedersen, J. S., ... & Haussler, D. (2006). An RNA gene expressed during cortical development evolved rapidly in humans. Nature, 443(7108), 167-172. (This study explores the rapid evolution of the HAR1 gene in humans, a gene expressed during cortical development.)

In this paper, Pollard and colleagues describe how the HAR1 region differs significantly between humans and chimpanzees. This is a concrete example of how even small genomic "edits" can lead to potentially profound differences in the biology and capabilities of two species. The changes in genes related to brain development, immunity, or metabolism result in radically different physiologies and capabilities. When observing the diverse modifications in the genomes of both humans and chimps, one can draw an analogy to two intricate pieces of machinery or sophisticated software applications. Each machine or software application is designed for a specific purpose. They might share some basic components or foundational code, but the specificities of their design show a targeted purpose. When a designer embarks on creating multiple products, he often uses a foundational template or set of core components to ensure efficiency and functionality. But it's the subtle variations, the nuanced differences, that reveal the true genius and intention behind each creation. These variations aren't random or accidental; they're deliberate, crafted with foresight for specific purposes. Consider the world of automobiles. Many cars share similar foundational components: engines, wheels, transmissions, and so forth. Yet, a sports car is distinct from an SUV not just in appearance but in function. The designer of the sports car envisions speed, aerodynamics, and performance, optimizing every part with that intent in mind. Conversely, the SUV is designed with space, ruggedness, and versatility at the forefront. Both vehicles stem from the basic concept of transportation, but their design specifics clearly reflect different purposes. Similarly, in the realm of software, a programmer might utilize the same base code to develop different applications. Yet, one application could be a sophisticated graphic design tool, while another could be a database management system. Both applications might contain similar foundational algorithms or libraries, but they have been intentionally modified and expanded upon to serve distinct functions. This analogy can be drawn closer to the genetic similarities and divergences seen between humans and chimps. Yes, they might share a foundational "code," but the precise "tweaks" and "modifications" in their DNA suggest distinct intentions for each. These aren't mere byproducts of chance but rather indications of a purposeful design. It's as though a mastermind, equipped with immense knowledge and foresight, has used a foundational template but introduced critical variations to ensure that each species is perfectly designed for the designer's goals and purpose.

Imagine two master engineers who, using their vast knowledge, craft two machines. Both machines have gears, circuits, and power sources, but one is tailored for deep-sea exploration, while the other is built for navigating the vastness of outer space. The sea-exploring machine is fitted with tools and sensors that allow it to withstand high pressure and detect changes in water composition. The space machine, on the other hand, is designed to operate in a vacuum, with radiation shields and equipment to analyze alien atmospheres. While they share fundamental design elements due to the engineers' shared knowledge, their specific and intricate modifications point towards an intentional design for distinct environments. In a similar vein, both humans and chimps might have genetic "tools" and "features" that suggest a certain foundational design principle. Still, the multitude of unique "edits" in their genomes are intentional modifications. It's as though the story of each species has been meticulously crafted, chapter by chapter, to ensure they thrive in their respective narratives, rather than being mere products of random or passive changes. If two books were being concurrently edited by the same author, you'd expect recent changes to be consistent between them. However, many of the recent "edits" in the human and chimp genomes are not shared, suggesting separate or independent origins.

Mobile Elements
Both species have "mobile elements" in their DNA, which can move around and create changes. Humans and chimps have different numbers and types of these stickers. Mobile elements, or transposons, are sequences in DNA that can change their position within the genome. Picture these as stickers in a scrapbook that, rather than being permanently affixed to a page, can move around and even duplicate themselves in the process. This movement can influence the function of genes, potentially leading to changes. When we compare the genomes of humans and chimps, one fascinating discovery is the shared insertion sites of some of these transposons. In other words, in both species, certain "stickers" are found in the same positions in their respective "scrapbooks." From an evolutionary standpoint, the shared sites are often cited as evidence for a common ancestry. The reasoning is that the odds of the same mobile element inserting itself independently at the exact same position in two separate species are extremely low. However, the shared insertion sites are indicative of a shared template or design plan. If we consider an architect who designs multiple buildings, it's plausible that certain features or designs are intentionally repeated across different structures because they serve a particular purpose or function. Similarly, the shared transposon sites reflect an intentional design element optimized for a specific function in both humans and chimps.

The shared transposon insertion sites between humans and chimps are primarily associated with classes of mobile elements like Alu sequences, LINEs, and SVA elements. These elements have been found at the same positions in the genomes of both species, Alu Sequences are short stretches of DNA (about 300 nucleotides long) that have proliferated to the extent that they make up about 10% of the human genome. In both humans and chimps, there are over a million copies of Alu sequences. A significant number of these are located at the same genomic positions in both species. While new Alu insertions can happen, the shared positions between humans and chimps can be intentionally placed markers.

The shared insertion sites have been mentioned and popularized as presenting a compelling case for shared ancestry from an evolutionary perspective. But there are alternative possible, plausible explanations. If the locations of these Alu insertions are crucial for some cellular or molecular function, then their shared presence in both human and chimp genomes is a feature of intentional design. Specific genomic loci might be "hotspots" for insertions because they offer functional advantages, such as influencing gene regulation or expression. If these sites provide a benefit, it makes sense that both humans and chimps have them, irrespective of common ancestry. Such insertions, found at the same relative location in both genomes, are powerful evidence for functionality when they have discernible roles in gene regulation or other genomic functions.

Several known functions of Alu elements include:

Influence on Gene Regulation: Alu elements can act as transcriptional enhancers or silencers, influencing the expression levels of nearby genes.
Alternative Splicing: Alu sequences in exons and introns influence alternative splicing patterns, resulting in diverse transcript variants. This can lead to the generation of various protein isoforms from a single gene.
Genomic Structural Variation: Alu elements can promote non-allelic homologous recombination events, which may result in genomic structural variations like deletions, duplications, and inversions.
Influence on Protein Coding: On rare occasions, parts of Alu sequences can be incorporated into mature mRNA and get translated, impacting protein function or creating novel peptides.
miRNA Target Sites: Alu elements can provide binding sites for microRNAs (miRNAs), small non-coding RNAs that regulate gene expression post-transcriptionally.
DNA Methylation: Alu elements can be sites for DNA methylation, an epigenetic modification that can influence gene expression. Alu-associated methylation can have implications in various biological processes, including aging and cancer.
Promotion of DNA Double-Strand Break Repair: There's evidence suggesting that Alu elements can participate in the DNA damage response, particularly in non-homologous end joining, a pathway for repairing DNA double-strand breaks.
Genome Evolution: Due to their repetitive nature and capacity for mobilization, Alu elements play a role in genome evolution by promoting genomic diversity.
Formation of Nuclear Domains: Alu elements have been implicated in the organization of certain nuclear domains which influence gene expression and other nuclear processes.
Stress Response: Some Alu elements are transcribed in response to various stresses, and their RNA products might play roles in cellular stress responses.
Source of Genetic Diseases: Mis-insertion or unequal recombination involving Alu elements can lead to genetic diseases.

Here's a notable paper on this topic:

Polak, P., & Domany, E. (2006). Alu elements contain many binding sites for transcription factors and may play a role in regulation of developmental processes. BMC Genomics, 7(1), 133. (This study explores the high frequency of transcription factor binding sites within Alu elements. Given that many of these Alu insertions are shared between humans and chimps, this study postulates that they may have roles in the regulation of developmental processes in both species.)

This paper not only sheds light on shared Alu insertions but also delves into their potential functional roles. The presence of shared insertion sites with functions like transcription factor binding suggests that these are not mere byproducts of random insertion events, but rather potentially conserved elements that play a role in the shared biology of humans and chimps.

There is also the observed influence of Alu sequences on gene regulation, expression, splicing, and other genomic functions. Influence on Gene Regulation and Expression:

Batzer, M. A., & Deininger, P. L. (2002). Alu repeats and human genomic diversity. Nature Reviews Genetics, 3(5), 370-379. (This comprehensive review highlights the impact of Alu sequences on genomic diversity and underscores their potential to influence gene expression and regulation.)

Sorek, R., Ast, G., & Graur, D. (2002). Alu-containing exons are alternatively spliced. Genome research, 12(7), 1060-1067. (This study demonstrates that Alu sequences within exons can influence alternative splicing patterns, leading to diverse transcript variants.)

Bejerano, G., Lowe, C. B., Ahituv, N., King, B., Siepel, A., Salama, S. R., ... & Haussler, D. (2006). A distal enhancer and an ultraconserved exon are derived from a novel retroposon. Nature, 441(7089), 87-90. (The paper identifies retroposon-derived sequences, including those similar to Alu elements, which have taken on critical regulatory roles in the human genome, particularly in neural gene expression.)

Each of these studies sheds light on the functional significance of Alu sequences, providing a plausible reason for their presence and conservation in specific genomic locations. These shared features are evidence for purposefully placed elements that contribute to the functionality and robustness of the genome.

Alu insertions
There are thousands of shared Alu insertions between humans and chimpanzees. Estimates suggest that humans and chimps share approximately 7,000 to 8,000 Alu element insertions. These shared insertions are often used as evidence in support of a common ancestor for the two species. Both evolution and design can operate under constraints. In the case of Alu insertions, there might be only a limited number of sites that are permissible or optimal for insertion. From a design perspective, these constraints could be imposed to ensure genomic stability, proper function, or other essential attributes. Hence, the presence of Alu sequences in the same loci across species are warranted to be seen as a feature of design operating within specific constraints, rather than evidence of common ancestry. If certain insertion sites offer advantages, it's possible that these sites could be chosen for both species due to their benefits, even without shared ancestry. The sheer complexity and intricate order of the genome might necessitate specific features to be in certain places. If one views the genome as a meticulously crafted system, then every part, including Alu insertions, has its designated place for the system to function optimally. The presence of these insertions in the same places in both species might be evidence of an underlying blueprint or pattern, much like how different models of a device might have components in the same locations because they are all based on a foundational design.

LINEs (Long Interspersed Nuclear Elements)
LINEs are longer sequences, typically around 6,000 nucleotides. LINE-1 (L1) is the most common type in mammalian genomes. There are shared L1 insertion sites between humans and chimps, again suggesting either a common ancestral origin or an intentional design. The idea of "hotspots" or preferred regions for transposable element insertions isn't new. These hotspots can be areas that are more accessible to the transposable element machinery, or they might be regions where insertion doesn’t result in a lethal effect, and thus these insertions can be passed on to the next generation.

Speek, M. (2001). Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes. Molecular and cellular biology, 21(6), 1973-1985. https://mcb.asm.org/content/21/6/1973
This study explores the regions where L1 elements integrate and suggests that certain genomic regions might be more conducive to these insertions due to their regulatory potential.

Boissinot, S., & Furano, A. V. (2001). Adaptive evolution in LINE-1 retrotransposons. Molecular biology and evolution, 18(12), 2186-2194. This paper discusses insights into the regions of the genome that might act as "hotspots" for LINE-1 insertions.

If L1 insertions were purely a result of common ancestry, the expectation would be that other closely related species would also share these same insertions. However, looking into the broader spectrum of primates and mammalian evolution, L1 activity and its patterns are not uniformly conserved across all lineages. Some key findings in various scientific studies have highlighted these discrepancies:

Salem, A. H. ... & Batzer, M. A. (2003). Alu elements and hominid phylogenetics. Proceedings of the National Academy of Sciences, 100(22), 12787-12791.
Link. (This paper explored Alu elements and their relevance in understanding hominid relationships. The study highlighted that the distribution of Alu elements is not always consistent with the accepted phylogenetic tree.)

Boissinot, S., Chevret, P., & Furano, A. V. (2000). L1 (LINE-1) retrotransposon evolution and amplification in recent human history. Molecular biology and evolution, 17(6), 915-928.
(This study on L1 elements showcases that the recent evolutionary amplification patterns of L1 are not consistent across all human populations.)

Khan, H., Smit, A., & Boissinot, S. (2006). Molecular evolution and tempo of amplification of human LINE-1 retrotransposons since the origin of primates. Genome research, 16(1), 78-87.
(This paper examined the evolutionary history of LINE-1 elements in humans and found that their amplification has not been steady over time and varies considerably among primates.)

Locke, D. P.... & Gibbs, R. A. (2011). Comparative and demographic analysis of orangutan genomes. Nature, 469(7331), 529-533.
(In this study, orangutan genomes were analyzed, revealing significant differences in the distribution and activity of mobile elements, including LINE-1, when compared to humans and other primates.)

These studies reveal that while there might be shared L1 insertions between humans and chimps, the broader context of primate evolution presents discrepancies. These discrepancies in shared L1 sites among a wider spectrum of primates indicate that there's more to the story than just a straightforward narrative of common ancestry based solely on L1 insertion similarity. If shared L1 insertion sites between humans and chimps have been demonstrated to serve essential regulatory or structural functions in the genome, it hints at an intentional design. Evolution by natural selection operates on functionality; it doesn't have foresight. In contrast, intentional design can place elements in anticipation of future needs or to serve intricate, multifaceted roles. The selection of studies presented covers a wide spectrum of the roles and implications of LINE-1 (L1) elements in the genome. At a holistic level, they make a compelling case that these elements are not mere genomic "junk" or arbitrary remnants of ancient viral insertions, but rather possess significant functionalities that might be better explained by a design perspective.

Speek (2001): The ability of the antisense promoter in the L1 retrotransposon to drive transcription of adjacent genes underscores the importance of L1 in influencing gene expression patterns. Such a feature can be likened to a regulatory mechanism, one that has been deliberately positioned to optimize the expression of essential genes. 1
Khan et al. (2006): If L1 elements were simply remnants of our evolutionary history, one would expect them to be uniformly amplified across primates. However, the study suggests that their amplification has been selective, hinting at some functional significance which has undergone specific pressures to maintain or change their presence. 2
Faulkner & Carninci (2009): Contrary to the notion that mobile elements like L1 are "selfish" and exist primarily for their propagation, this research elucidates their "altruistic" roles that benefit the host. Such complex dual roles—both selfish and altruistic—are indicative of a design with multifaceted purposes.3
de Koning et al. (2011): The staggering presence of repetitive elements in the human genome, including L1, challenges the idea that these sequences are merely evolutionary leftovers. Their abundance suggests an orchestrated design, with each element playing a part in the genomic symphony. 4
Fort et al. (2014): The involvement of retrotransposons, including L1, in maintaining pluripotency of mammalian stem cells, is a testament to their essential function. It's challenging to dismiss such a pivotal role as a mere coincidence arising from shared ancestry.5
Lewinski & Bushman (2005): By diving into the mechanics and implications of retroviral DNA integrations akin to L1, this review encapsulates the myriad ways through which these elements impact genomic structure and function. The precision and intricacy of these mechanisms point towards a well-calibrated system, which could be seen as a hallmark of design.6

The genome operates as a complex system with multiple layers of regulation and interaction. Shared L1 insertions that are found in functionally crucial regions of the genome (e.g., gene regulatory networks) in both species can be seen as evidence of a shared design template. Just as an engineer might use a specific component in multiple devices because of its reliability and function, the shared L1 sites can be viewed as essential components in the genomic machinery. If the shared L1 insertions work in coherence with other genomic elements (like Alu sequences or specific genes) in a way that creates a harmonized system in both humans and chimps, it would suggest a design principle that values integration and harmony in genomic operations.

SVA Elements
These are newer, composite elements made up of sequences from other transposons. They're called SVAs because they contain segments from SINEs, VNTRs, and Alu sequences. While there are fewer SVAs than Alus or LINEs, shared insertion sites can still be found between humans and chimps.

Additionally, it's essential to note that while many insertion sites are shared, there are also numerous sites unique to each species, highlighting the distinctiveness of their genetic makeup. These unique sites, along with the shared ones, contribute to the overall complexity and specificity of each species' genome.

Gene Differences
The genes, or instruction sets, for things like smell (olfactory receptors) differ between the two species. Both have unique mutations in genes that deal with immune responses and how cells recognize each other. Humans have specific mutations related to speech and brain size, while chimps have their own unique mutations. Apart from genes that instruct how to build and operate a body, there are other DNA segments, "non-coding sequences", that help control how these genes work. Humans have special regions called HARs and HACNs. These areas are especially important for brain development and function. Both species have various pericentric inversions, as well as a multitude of deletions, insertions, and copy number variations. The complexity and multitude of these alterations suggest separate genetic pathways and histories, rather than modifications from a shared ancestor. There are species-specific mutations and differing repertoires of genes related to olfaction, immunity, sialic acids metabolism, and brain development. The unique genes and mutations in each species might suggest they were crafted for specific purposes, hinting at separate origins. Differences exist in the coding sequences of both species, such as the divergent genes related to immunity and cell recognition. The unique sets of protein-coding genes in each species may imply separate genetic blueprints, supporting the idea of separate origins.

Neurological Distinctions
Humans have unique white matter tracts, with changes in their architecture, implying different neural connections. This impacts cognitive functions and our ability for abstract thinking, planning, and complex language.
Distinct genes related to neurotransmitters affect behavior, cognition, and social interactions differently in the two species.

White Matter Tracts and Cognitive Function
Human brains show a distinctive pattern of myelination, particularly in the white matter tracts. Myelin is crucial for rapid signal transmission in neural pathways. Enhanced myelination in humans, especially in the frontal lobes, contributes to quicker cognitive processing and advanced decision-making capabilities. Arcuate Fasciculus is a white matter tract connecting the Broca's area and the Wernicke's area in the human brain, essential for language comprehension and production. While chimps do have an arcuate fasciculus, it's less developed and doesn't have the same connectivity, which may partly explain why they don't possess complex language capabilities like humans.

The Significance of the Arcuate Fasciculus AF in Humans
The AF is not just a simple connector between Broca's and Wernicke's areas, but serves as an essential highway for a plethora of linguistic processes. This includes semantics (meaning), syntax (sentence structure), prosody (intonation and rhythm), and phonological processing. The development and sophistication of the AF in humans facilitates the nuanced and multifaceted nature of our language. Research using diffusion tensor imaging has revealed that the human AF consists of both anterior-to-posterior and posterior-to-anterior segments, indicating a bidirectional flow of information. This two-way communication is essential for the real-time feedback and rapid processing required for fluent speech and comprehension. Beyond just Broca's and Wernicke's areas, the AF interacts with other parts of the brain, such as the inferior parietal lobule, involved in tasks like reading and number processing. This suggests its role in integrating diverse cognitive functions, not just speech. The level of sophistication and intricacy in the human AF, compared to its simpler counterpart in chimps, doesn't lend itself easily to gradual evolutionary narratives. It's hard to envision intermediary stages where a partially formed AF would offer significant evolutionary advantages. For the AF to evolve to support language, language itself would need to co-evolve with the tract. This simultaneous evolution of brain structures and sophisticated linguistic capabilities presents a chicken-and-egg problem. Which came first: the linguistic need or the neural structure? If the AF in earlier hominins or common ancestors of humans and chimps was underdeveloped (similar to chimps), they would likely have alternative neural pathways for communication. Evolutionary development of the AF would render these pathways redundant, which is inefficient from an evolutionary perspective. The AF's intricate architecture in humans, with its bidirectional pathways and connections to multiple brain regions, suggests a purposeful design tailored for complex linguistic and cognitive tasks. This is less about a mere enlargement or modification of an existing structure and more about a reimagining of its role and capabilities. The disparity in the development and functionality of the AF between humans and chimps indicates distinct blueprints or origins, rather than one species being a modified version of the other. The brain operates as a holistic network. A change in one area (like the AF) can impact various other regions and functions. The seamless integration of the AF in the human neural framework underscores the idea of a coordinated and thoughtfully crafted design, as opposed to haphazard evolutionary additions.

Corpus Callosum Connectivity
The corpus callosum in humans supports enhanced interhemispheric communication, critical for complex tasks like reading and abstract thinking. Chimps, while having a corpus callosum, exhibit differences in their architecture and function. The corpus callosum is the largest white matter tract in the human brain and plays a pivotal role in integrating functions of the left and right cerebral hemispheres. Its intricate design in humans compared to other primates like chimps raises profound questions about the nature and origin of its development. The corpus callosum facilitates rapid and complex communication between the two hemispheres. This integration enables humans to perform tasks that require the simultaneous engagement of both hemispheres, such as understanding metaphors, where the left hemisphere processes the language and the right processes the abstract concept. Motor and Sensory Integration plays a role in coordinating motor outputs and sensory inputs between the hemispheres. This is evident in tasks requiring hand-eye coordination, where both hemispheres must work in tandem. The right hemisphere plays a significant role in processing emotions. Through the corpus callosum, emotional signals can be rapidly transferred and processed in the context of language and logic located predominantly in the left hemisphere.

While chimps have a corpus callosum, there are distinctions: The human corpus callosum, when adjusted for brain size, is thicker and contains more axons. This means more information can be transferred and at a quicker rate in humans. The patterns of connectivity, and thus the specific functions facilitated by the corpus callosum in chimps, may be different from those in humans, reflecting the disparate cognitive capabilities between the species.
Given the profound impact of the corpus callosum on human cognition and its intricate design, it's challenging to envision intermediary stages of its evolutionary development where incremental advantages would be provided.
The brain isn't just about having connections, but about having the right ones. For every neuron in the brain, there are approximately 10,000 synaptic connections to other neurons. The mathematical permutations for these connections are staggering. Even a slight miswiring could lead to non-functionality or malfunctions. A fully functional corpus callosum emerging through random mutations seems immensely improbable. The evolution of the corpus callosum's advanced design would necessitate the simultaneous evolution of other brain regions and functionalities that it interfaces with. Such a synchronized evolution poses a significant challenge to explain. The precise and meticulous design of the human corpus callosum points to intentional crafting. Its integration with other brain areas seems purposefully coordinated for complex cognitive functions. The capabilities facilitated by our corpus callosum, like abstract thinking, are uniquely human. Such distinctive features hint at a separate origin or blueprint rather than an incremental development from a primate ancestor.

Neurotransmitters and Behavior
The DRD4 gene, which codes for the dopamine receptor, has variations in humans linked with novelty-seeking behavior. Chimps have different versions of this gene, leading to differences in risk-taking and exploratory behavior.
Variations in genes regulating serotonin can influence social behavior. Humans have specific genes that underpin our cooperative nature and societal structures, while chimps possess versions that support their more hierarchical and territorial social systems. HARs (Human Accelerated Regions) are segments of the genome that are often involved in gene regulation, especially during brain development. microRNAs are small RNA molecules that play a crucial role in gene regulation. Humans and chimps have differences in the expression and function of several microRNAs, especially those implicated in brain function and development. Methylation patterns, an epigenetic mechanism, can vary between humans and chimps. Differences in these patterns can influence how genes are turned on or off, leading to divergence in traits and functionalities. Gene regulatory networks often involve feedback loops, where the product of a gene can influence its own expression or that of other genes. Differences in these loops between the species can lead to a cascade of changes, drastically altering biological outcomes. Given the complexity of these networks, even minor initial differences imply in significant divergence. While humans and chimps share a substantial portion of their DNA, the intricate differences in neural architecture, neurotransmitter regulation, and gene regulatory networks strongly suggest separate evolutionary trajectories. These distinct pathways and the resulting differences in cognition, behavior, and social structures provide powerful evidence against a singular shared ancestry.

Further differences
Humans and chimps have different dietary requirements and digestion mechanisms. Chimps have a more robust gut to process a varied diet, including raw plant materials, whereas humans are adapted to eat cooked food. Chimps have unique genes catering to their knuckle-walking motion, while humans possess genetic codes for upright bipedalism, affecting everything from our pelvis structure to foot arches. Humans have an extended childhood and adolescence phase compared to chimps. Genetic differences dictate the human brain's slower maturation and our longer reproductive cycle. The genetic, epigenetic, manufacturing, and regulatory information and signaling pathways and information result in different lengths of pregnancies between the two species, with humans having a notably longer gestation period. While both rely heavily on vision, humans have specific genes related to trichromatic vision, aiding in discerning a broader spectrum of colors. Chimps, although having good vision, don't have the same color discernment abilities. Genetic differences result in variations in taste bud receptors. For instance, humans are sensitive to a broader range of tastes, making us more discerning eaters. Interestingly, chimps have a faster wound-healing process than humans. Distinct genetic pathways provide them with a more efficient recovery mechanism.
While humans might be susceptible to certain diseases, chimps might be naturally immune to them, and vice-versa. This can be attributed to species-specific immune-related genes. Differences in DNA methylation, a mechanism used to control gene expression, between humans and chimps points to different evolutionary trajectories. Studies suggest that certain genes mutate at different rates in humans and chimps, indicating separate evolutionary trajectories.

1. Speek, M. (2001). Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes. Molecular and Cellular Biology, 21(6), 1973-1985. Link.
This paper demonstrates that the antisense promoter in the L1 retrotransposon can drive the transcription of adjacent cellular genes. This shows that L1 can influence gene expression patterns.
2. Khan, H., Smit, A., & Boissinot, S. (2006). Molecular evolution and tempo of amplification of human LINE-1 retrotransposons since the origin of primates. Genome research, 16(1), 78-87. Link.
This study reveals that LINE-1 elements, such as L1, have not been uniformly amplified across primate evolution. Their distribution and activity patterns suggest selective pressures, indicating their potential functional significance.
3. Faulkner, G. J., & Carninci, P. (2009). Altruistic functions for selfish DNA. Cell cycle, 8(18), 2895-2900. Link.
This study showcases the broader perspective that mobile elements, including L1, have roles beyond "selfish" propagation. They often have "altruistic" roles beneficial for the host organism, like gene regulation.
4. de Koning, A. P., Gu, W., Castoe, T. A., Batzer, M. A., & Pollock, D. D. (2011). Repetitive elements may comprise over two-thirds of the human genome. PLoS genetics, 7(12), e1002384. Link.
This comprehensive study suggests that a significant portion of the human genome is comprised of repetitive elements, including L1. The sheer abundance of these elements points towards their potential functionality.
5. Fort, A., Hashimoto, K., Yamada, D., Salimullah, M., Keya, C. A., Saxena, A., ... & Carninci, P. (2014). Deep transcriptome profiling of mammalian stem cells supports a regulatory role for retrotransposons in pluripotency maintenance. Nature genetics, 46(6), 558-566. Link.
This study provides a deep insight into the transcriptional profile of mammalian stem cells. It supports the idea that retrotransposons, including L1, play a role in maintaining pluripotency.
6. Lewinski, M. K., & Bushman, F. D. (2005). Retroviral DNA integration—mechanism and consequences. Advances in genetics, 55, 147-181. Link.
This review covers the mechanics and consequences of retroviral DNA integration, including elements similar to L1. It underscores the potential functional implications of such insertions.



////Point out, why a nonguided, non-intelligent set-up, step by step, is extremely unlikely, and design a far more case-adequate explanation of each point. write from the perspective of a proponent of intelligent design. Do not write: " From an intelligent design standpoint ". Just say it.Do not put enumeration numbers at the beginning of the sentences. Write in bbcode, like this:

The Mathematical Order in the Laws of Physics: The universe is governed by several fundamental laws of physics, which can be expressed with high precision using mathematical equations. From Newton's laws of motion to Einstein's theory of relativity, these equations predict the behavior of objects and energy within our universe. The universality and consistency of these laws suggest a deep-rooted structure in the fabric of reality.[/size] Their universal applicability, from the movement of galaxies to subatomic particles, points to a harmonized system rather than a chaotic one. The probability of such exact and universally applicable laws emerging from randomness is vanishingly low. The precision of gravitational constants, the speed of light, or Planck's constant, to name a few, doesn't merely offer predictability; they shape the very conditions necessary for life and the stability of the universe as we know it. A slight deviation in any of these constants could render the universe hostile or chaotic. The fine-tuning required for these constants to align in a way that supports structured cosmic evolution and life appears beyond the scope of sheer chance. Furthermore, the emergence of mathematical equations that can accurately describe these laws hints at a profound relationship between the physical world and the abstract realm of mathematics. Why should the universe, if borne out of randomness, adhere so faithfully to mathematical descriptions? The inherent order and mathematical structure suggest that there is a foundational logic and design to the universe. When we explore phenomena like quantum entanglement or the conditions necessary for the Big Bang, the interconnectedness and sensitivity of these systems seem to defy unguided emergence. Instead, the cohesive framework of physical laws, coupled with their mathematical elegance, makes the argument for an underlying intelligence overwhelmingly compelling. Given the depth of order, precision, and fine-tuning in the laws of physics, attributing their existence to mere chance seems foolish and nonsensical. The very fabric of our reality, woven with these laws, appears to resonate with the signs of purposeful design.



1. Something new created based on no pre-existing physical conditions or state of affairs ( a concept, an idea, a plan, a project, a blueprint)
2. A specific functional state of affairs, based on and dependent on mathematical rules, that depend on specified values ( that are independent, nonconditional, and that have no deeper grounding)
3. A force/cause that secures, upholds, maintains, and stabilizes a state of affairs, avoiding stochastic chaos. Eliminating conditions that change unpredictably from instant to instant or preventing things from uncontrollably popping in and out of existence.
4. Fine-tuning or calibrating something to get the function of a (higher-order) system.
5. Selected specific materials, that have been sorted out, concentrated, and joined at a construction site.
6. An information storage system ( paper, a computer hard disk, etc.)
7. A language, based on statistics, semantics, syntax, pragmatics, and apobetics
8. A code system, where meaning is assigned to characters, symbols, words
9. Translation ( the assignment of the meaning of one word in one language to another of another language ) that has the same meaning
10. An information transmission system ( a radio signal, internet, email, post delivery service, etc.)
11. A plan, blueprint, architectural drawing, or scheme for accomplishing a goal, that contains instructional information, directing the making for example of a 3D artifact, 1:1 equivalent to the plan of the blueprint.
12. Conversion ( digital-analog conversion, modulators, amplifiers)
13. Overlapping codes ( where one string of information can have different meanings)
14. Systems of interconnected software and hardware
15. A library index and fully automated information classification, storage, and retrieval program
16. A software program that directs the making, and governs the function or/and operation of devices with specific functions.
17. Energy turbines
18. To create, execute, or construct something precisely according to an instructional plan or blueprint
19. The specific complex arrangement and joint of elements, parts, or materials to create a machine or a device for specific functions
20. A machine, that is, a piece of equipment with several moving parts that uses power to do a particular type of work that achieves a specific goal
21. Repetition of a variety of complex actions with precision based on methods that obey instructions, governed by rules.
22. Preprogrammed production or assembly lines that employ a series of machines/robots in the right order that are adjusted to work in an interdependent fashion to produce a specific functional (sub) product.
23. Factories, that operate autonomously in a preprogrammed manner, integrating information that directs functions working in a joint venture together.
24. Objects that exhibit “constrained optimization.” The optimal or best-designed laptop computer is the one that has the best balances and compromise of multiple competing factors.
25. Artifacts which use might be employed in different systems (a wheel is used in cars and airplanes)
26. Error monitoring, check, and repair systems, depending on recognizing when something is broken, identifying where exactly the object is broken, to know when and how to repair it (e.g. one has to stop/or put on hold some other ongoing processes; one needs to know lots of other things, one needs to know the whole system, otherwise one creates more damage…) to know how to repair it (to use the right tools, materials, energy, etc, etc, etc ) to make sure that the repair was performed correctly.
27. Defense systems based on data collection and storage to protect a system/house, factory, etc. from invaders, intruders, enemies, killers, and destroyers.
28. Sending specific objects from address A to address B based on the address provided on the object, which informs its specific target destination.
29. Keeping an object in a specific functional state of affairs as long as possible through regulation, and extending the duration upon which it can perform its task, using monitoring, guaranteeing homeostasis, stability, robustness, and order.
30. Self-replication of a dynamical system that results in the construction of an identical or similar copy of itself. The entire process of self-replication is data-driven and based on a sequence of events that can only be instantiated by understanding and knowing the right sequence of events. There is an interdependence of data and function. The function is performed by machines that are constructed based on the data instructions. (Source: Wikipedia)
31. Replacing machines, systems, etc. in a factory before they break down as a preventive measure to guarantee long-lasting functionality and stability of the system/factory as a whole.
32. Recycling, which is the process of converting waste materials into new materials and objects. The recovery of energy from waste materials is often included in this concept. The recyclability of a material depends on its ability to reacquire the properties it had in its original state. ( Source: Wikipedia)
33. Instantiating waste management or waste disposal processes that include actions required to manage waste from its inception to its final disposal. This includes the collection, transport, treatment, and disposal of waste, together with monitoring and regulation of the waste management process. ( Source: Wikipedia)
34. Electronic circuits are composed of various active functional components, such as resistors, transistors, capacitors, inductors, and diodes, connected by conductive wires through which electric current can flow. The combination of components and wires allows various simple and complex operations to be performed: signals can be amplified, computations can be performed, and data can be moved from one place to another. (Source: Wikipedia)
35. Arrangement of materials and elements into details, colors, and forms to produce an object or work of art able to transmit the sense of beauty, and elegance, that pleases the aesthetic senses, especially sight.
36. Instantiating things on the nanoscale. Know-how is required in regard to quantum chemistry techniques, chemical stability, kinetic stability of metastable structures, the consideration of close dimensional tolerances, thermal tolerances, friction, and energy dissipation, the path of implementation, etc. See: Richard Jones: Six challenges for molecular nanotechnology December 18, 2005
37. Objects in nature very similar to human-made things // point out, why these things are indicative of intelligent design, and not unguided, non-intelligent, natural events.

Indicative of Intelligent Design:

Something new created based on no pre-existing physical conditions or state of affairs (a concept, an idea, a plan, a project, a blueprint): This demonstrates the ability to conceive and plan, attributes of intelligent design.
A specific functional state of affairs, based on and dependent on mathematical rules, that depend on specified values (that are independent, nonconditional, and that have no deeper grounding): Mathematical precision suggests a deliberate design.
A force/cause that secures, upholds, maintains, and stabilizes a state of affairs, avoiding stochastic chaos: Intelligent design is needed to establish and maintain stability.
Fine-tuning or calibrating something to get the function of a (higher-order) system: This precision indicates a thoughtful design process.
Selected specific materials, that have been sorted out, concentrated, and joined at a construction site: The selection and concentration of materials require a deliberate choice.
An information storage system (paper, a computer hard disk, etc.): Designing systems for storing information is an intelligent process.
A language, based on statistics, semantics, syntax, pragmatics, and apobetics: The complexity of language implies intelligent design.
A code system, where meaning is assigned to characters, symbols, words: Assigning meaning to symbols is a product of intelligent design.
Translation (the assignment of the meaning of one word in one language to another of another language) that has the same meaning: Accurate translation involves understanding and design.
An information transmission system (a radio signal, internet, email, post delivery service, etc.): Designing systems for information transmission is an intelligent act.
A plan, blueprint, architectural drawing, or scheme for accomplishing a goal, that contains instructional information, directing the making, for example, of a 3D artifact, 1:1 equivalent to the plan of the blueprint: Planning and blueprinting are quintessential examples of intelligent design.
Conversion (digital-analog conversion, modulators, amplifiers): Engineering conversions indicate intelligent design.
Overlapping codes (where one string of information can have different meanings): Complex coding systems require intelligent design.

Systems of interconnected software and hardware: The integration of software and hardware requires intelligent engineering.

A library index and fully automated information classification, storage, and retrieval program: Creating systems to organize and retrieve information is an intelligent design task.

A software program that directs the making and governs the function or/and operation of devices with specific functions: Developing software to control devices demonstrates intelligent design.

Energy turbines: The design of energy turbines showcases intelligent engineering.

To create, execute, or construct something precisely according to an instructional plan or blueprint: Following a blueprint is an act of intelligent execution.

The specific complex arrangement and joint of elements, parts, or materials to create a machine or a device for specific functions: Complex arrangements signify intelligent engineering.

A machine, that is, a piece of equipment with several moving parts that uses power to do a particular type of work that achieves a specific goal: Designing machines is a clear sign of intelligent engineering.

Repetition of a variety of complex actions with precision based on methods that obey instructions, governed by rules: Precise repetition of complex actions requires intelligent design.

Preprogrammed production or assembly lines that employ a series of machines/robots in the right order that are adjusted to work in an interdependent fashion to produce a specific functional (sub) product: Setting up preprogrammed production lines is an intelligent design process.

Factories, that operate autonomously in a preprogrammed manner, integrating information that directs functions working in a joint venture together: Designing autonomous factories demonstrates intelligent planning.

Objects that exhibit “constrained optimization.” The optimal or best-designed laptop computer is the one that has the best balances and compromise of multiple competing factors: Achieving constrained optimization is a product of intelligent design.

Artifacts which use might be employed in different systems (a wheel is used in cars and airplanes): The adaptability of artifacts indicates intelligent design.

Error monitoring, check, and repair systems, depending on recognizing when something is broken, identifying where exactly the object is broken, to know when and how to repair it: Designing systems for error monitoring and repair involves intelligent planning.

Defense systems based on data collection and storage to protect a system/house, factory, etc. from invaders, intruders, enemies, killers, and destroyers: Defensive systems involve intelligent design to protect against threats.

Sending specific objects from address A to address B based on the address provided on the object, which informs its specific target destination: This requires intelligent logistics.

Keeping an object in a specific functional state of affairs as long as possible through regulation, and extending the duration upon which it can perform its task, using monitoring, guaranteeing homeostasis, stability, robustness, and order: Maintaining functionality and order is a result of intelligent design.

Self-replication of a dynamical system that results in the construction of an identical or similar copy of itself: Self-replication involves a sequence of events and interdependence of data and function, indicating intelligent design.

Replacing machines, systems, etc. in a factory before they break down as a preventive measure to guarantee long-lasting functionality and stability of the system/factory as a whole: Preventive maintenance demonstrates intelligent planning.

Recycling, which is the process of converting waste materials into new materials and objects: Recycling involves controlled processes, suggesting intelligent design.

Instantiating waste management or waste disposal processes that include actions required to manage waste from its inception to its final disposal: Managing waste is a deliberate process, not a result of random events.

Electronic circuits are composed of various active functional components, such as resistors, transistors, capacitors, inductors, and diodes: Designing electronic circuits is an example of intelligent engineering.

Arrangement of materials and elements into details, colors, and forms to produce an object or work of art able to transmit the sense of beauty and elegance, that pleases the aesthetic senses, especially sight: Artistic arrangement reflects intelligent design.

Instantiating things on the nanoscale: Nanoscale engineering involves precise design and knowledge of quantum chemistry.



Last edited by Otangelo on Thu Oct 26, 2023 6:48 am; edited 1 time in total

https://reasonandscience.catsboard.com

319Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Oct 25, 2023 12:16 pm

Otangelo


Admin

/// rewrite the list, focussing exclusively on players, that are involved in quality control, error-check, repair, discard and recycling from the given list, and not adding anything else. That includes proteins, signaling pathways, and everything else. Players exclusively used in the maturation and biosynthesis of the ribosome itself are treated elsewhere. This is about the monitoring process during translation of any protein. keep the same format, bbcode. Do not change the format without advice. In this format:
Do not repeat if you have listed these players previously.

Quality Control, Error-Check, Repair, Discard, and Recycling during Prokaryotic Translation

Ribosome Stalling and Rescue:
tmRNA: Recognizes stalled ribosomes and facilitates their rescue.
SmpB: Works with tmRNA to rescue stalled ribosomes.
ArfA and ArfB (YaeJ): Ribosome rescue proteins active when tmRNA is absent or non-functional.

Proteolytic Systems for Truncated Peptides:
Lon Protease: Degrades polypeptides tagged by tmRNA.
ClpXP Protease: Another protease system for degrading tagged peptides.

https://reasonandscience.catsboard.com

320Perguntas .... - Page 13 Empty Re: Perguntas .... Thu Oct 26, 2023 2:22 pm

Otangelo


Admin

Mechanisms that identify mistakes or issues during the actual protein synthesis process.

Prokaryotic-Exclusive Mechanisms

Overview of the quality control, error-check, repair, discard, and recycling mechanisms during prokaryotic translation.

1. Ribosome Stalling and Rescue
Key Players:
tmRNA: Recognizes stalled ribosomes and facilitates their rescue.
SmpB: Works with tmRNA to rescue stalled ribosomes.
ArfA and ArfB (YaeJ): Ribosome rescue proteins active when tmRNA is absent or non-functional.

2. Proteolytic Systems for Truncated Peptides
Key Players:
Lon Protease: Degrades polypeptides tagged by tmRNA.
ClpXP Protease: Another protease system for degrading tagged peptides.

3. RNA Quality Control for Faulty mRNAs
Key Players:
RNase R: Exoribonuclease that degrades faulty mRNA.
PNPase: Another ribonuclease involved in faulty mRNA degradation.
RNase II: Degradation of defective mRNA.

4. Translation Error-Check and Repair
Key Players:
EF-Tu: Ensures accurate aminoacyl-tRNA delivery to prevent mismatches.
RelA and SpoT: Detect amino acid starvation and trigger the stringent response to reduce errors.
5. Ribosome Collision and Quality Control
Key Players:

HflX: GTPase involved in dissociating collided or stalled ribosomes.
RsfA: Involved in preventing elongation in specific contexts to avoid errors.

6. Other Quality Control and Regulatory Factors
Key Players:
RqcH and RqcP: Address stalled translation events.
YbeY: Ribosome quality control via its endonuclease activity.
MazEF: Toxin-antitoxin system; regulates translation under stress.

7. Chaperones for Folding and Protein Quality
Key Players:
DnaK/DnaJ/GrpE: Chaperone system to aid in protein folding, especially for those emerging from the ribosome.
GroEL/GroES: Major chaperone system assisting newly synthesized polypeptides.

8. tmRNA-Mediated Ribosome Rescue
Key Players:
tmRNA, SmpB protein.
Pathway: tmRNA with SmpB acts as both tRNA and mRNA, adding a peptide tag to the nascent chain for proteolysis.

9. Trans-Translation
Key Players:
tmRNA, SmpB.
Pathway: Similar to tmRNA-mediated ribosome rescue, but can also result in mRNA cleavage.

10. Lon and Clp Proteases
Key Players:
Lon protease, ClpXP, ClpAP.
Pathway: Recognizes and degrades irregular peptides to maintain protein homeostasis.


Eukaryotic-Exclusive Mechanisms

Insight into the quality control, error correction, repair, and degradation mechanisms during eukaryotic translation.

1. Degradation of Faulty mRNAs
Key Players:
RNase II and RNase R: Exoribonucleases that target problematic mRNAs for degradation.
PNPase: Degrades aberrant rRNA and mRNA molecules.

2. Ribosomal Recycling
Key Players:
RRF (Ribosome Recycling Factor): Assists in disassembling ribosomal subunits after translation.

3. Error Correction in Aminoacylation
Key Players:
Editing domains of Aminoacyl-tRNA synthetases: Ensure tRNA charging accuracy by hydrolyzing incorrectly charged tRNAs.
YbaK: Provides an additional layer of fidelity for prolyl-tRNA.

4. E-site Regulation
Key Players:
Elongation factors (EF-Tu and EF-G): Regulate tRNA movement through the ribosomal sites, especially the exit (E-site).

5. Degradation of Misfolded Proteins
Key Players:
DegP (HtrA): Targets misfolded proteins in the periplasm for degradation.
ClpB and the DnaK/DnaJ/GrpE chaperone system: Either refold or target misfolded proteins for degradation.

6. Ribosomal Surveillance
Key Players:
RsfA: Oversees ribosome integrity and directs any damaged ribosomes towards degradation.
Rne and Rng: Act in quality control by cleaving problematic RNA sequences.

7. Recognition of Stalled Ribosomes and Nascent Chain Issues
Key Players:
RQC complex: Identifies stalled ribosomes and collaborates with downstream elements for resolution.
DnaK and DnaJ in prokaryotes (similar to Hsp70 and Hsp40 in eukaryotes): Bind to and aid in the refolding or disposal of misfolded proteins.

8. Disaggregation and Refolding of Problematic Polypeptides
Key Players:
Hsp100/Clp family: Solubilizes aggregated proteins, making them accessible for refolding chaperones.

9. Targeting for Degradation
Key Players:
ATP-dependent proteases in prokaryotes: Degrade misfolded or problematic polypeptides without a need for prior tagging.

10. Stress Response Triggered by Translation Errors
Key Players:
Heat shock response: Enhances the expression of chaperones and proteases to manage misfolded proteins during increased protein misfolding or stress conditions.


Mechanisms Shared by Both Prokaryotic and Eukaryotic Cells

Insight into the conserved quality control, error correction, and degradation mechanisms across both prokaryotic and eukaryotic translation.

1. Aminoacyl-tRNA Synthetases with Editing Domains
Key Players:
AARSs: Charge tRNAs with appropriate amino acids, ensuring translation accuracy.
Editing Domains: Provide a secondary quality control, hydrolyzing wrongly charged tRNAs.

2. Elongation Factors
Key Players:
Prokaryotes: EF-Tu, EF-G.
Eukaryotes: Analogous elongation factors.
Pathway: Mediate the movement of tRNAs through ribosomal sites, ensuring smooth translation.

3. Ribosome Structure and Function
Overview:
Fundamental ribosome structure and functions are conserved across domains.
Core mechanisms, especially rRNA-mediated peptide bond formation, remain consistent.

4. Molecular Chaperones
Key Players:
Prokaryotes: DnaK/DnaJ.
Eukaryotes: Hsp70/Hsp40.
Function: Aid in correct protein folding or target misfolded proteins for degradation.

5. ATP-dependent Proteases
Overview:
Both cellular types utilize ATP-dependent proteases to degrade damaged or misfolded proteins.

6. tRNA Modifications
Overview:
Modifications, especially at the tRNA's anticodon loop, ensure accuracy in translation across both domains.

7. Heat Shock Response
Overview:
Both prokaryotes and eukaryotes upregulate specific proteins to manage misfolded proteins during stress conditions.

8. Ribosome Recycling
Overview:
After translation completion, both domains dissociate ribosomes from mRNA for recycling.

9. Quality Control of mRNA
Key Players:
Exoribonucleases: RNase II and RNase R.
Function: Degrade problematic mRNAs in both prokaryotes and eukaryotes.

The shared mechanisms emphasize the importance and universal requirement for accurate translation of genetic information into functional proteins across all life forms.

Prokaryotic Error Detection during Translation:

Ribosome Stalling and Rescue: 4 proteins (tmRNA, SmpB, ArfA, ArfB)
Proteolytic Systems for Truncated Peptides: 3 proteins (Lon Protease, ClpXP Protease, ClpAP)
RNA Quality Control for Faulty mRNAs: 3 proteins (RNase R, PNPase, RNase II)
Translation Error-Check and Repair: 3 proteins (EF-Tu, RelA, SpoT)
Ribosome Collision and Quality Control: 2 proteins (HflX, RsfA)
Other Quality Control and Regulatory Factors: 4 proteins (RqcH, RqcP, YbeY, MazEF)
Chaperones for Folding and Protein Quality: 4 proteins (DnaK, DnaJ, GrpE, GroEL/GroES)
tmRNA-Mediated Ribosome Rescue: 2 proteins (tmRNA, SmpB)
Trans-Translation: 2 proteins (tmRNA, SmpB)
Lon and Clp Proteases: 3 proteins (Lon protease, ClpXP, ClpAP)
Total for Prokaryotic: 32 proteins

Eukaryotic Error Detection during Translation:

Degradation of Faulty mRNAs: 3 proteins (RNase II, RNase R, PNPase)
Ribosomal Recycling: 1 protein (RRF)
Error Correction in Aminoacylation: 2 proteins (Editing domains of Aminoacyl-tRNA synthetases, YbaK)
E-site Regulation: 2 proteins (EF-Tu, EF-G)
Degradation of Misfolded Proteins: 3 proteins (DegP, ClpB, DnaK/DnaJ/GrpE chaperone system)
Ribosomal Surveillance: 3 proteins (RsfA, Rne, Rng)
Recognition of Stalled Ribosomes and Nascent Chain Issues: 3 proteins (RQC complex, DnaK, DnaJ)
Disaggregation and Refolding of Problematic Polypeptides: 1 protein (Hsp100/Clp family)
Targeting for Degradation: 1 protein (ATP-dependent proteases in prokaryotes)
Stress Response Triggered by Translation Errors: 1 protein (Heat shock response)
Nonsense-Mediated Decay (NMD): 8 proteins (UPF1, UPF2, UPF3, SMG1-7)
No-Go Decay (NGD): 2 proteins (Dom34/Pelota, Hbs1)
Non-Stop Decay (NSD): 1 protein (Ski7/Hbs1 and Pelota)
Ribosome-Associated Quality Control (RQC): 3 proteins (LTN1, NEMF, TCF25)
mRNA Surveillance: 4 proteins (eIF4A3, MAGOH, Y14, MLN51)
Endoplasmic Reticulum (ER)-Associated Degradation (ERAD): 4 proteins (EDEM, HERP, SEL1L, HRD1)
Chaperone-Assisted Protein Quality Control: 3 proteins (HSP70, HSP90, CHIP)
Total for Eukaryotic: 47 proteins

Error Detection Mechanisms in Translation Extant in Both, Prokaryotes and Eukaryotes:

Aminoacyl-tRNA Synthetases with Editing Domains: 2 features (AARSs, Editing Domains)
Elongation Factors: Prokaryotes - 2 proteins (EF-Tu, EF-G), Eukaryotes - at least 2 proteins (analogous elongation factors)
Ribosome Structure and Function: 1 feature (Fundamental ribosome structure and functions)
Molecular Chaperones: Prokaryotes - 2 proteins (DnaK, DnaJ), Eukaryotes - 2 proteins (Hsp70, Hsp40)
ATP-dependent Proteases: 1 feature (ATP-dependent proteases in both cellular types)
tRNA Modifications: 1 feature (tRNA's anticodon loop modifications)
Heat Shock Response: 1 feature (Upregulation of specific proteins in response to stress)
Ribosome Recycling: 1 feature (Ribosome dissociation from mRNA after translation)
Quality Control of mRNA: Prokaryotes - 2 proteins (RNase II, RNase R), Eukaryotes - at least 1 protein system (exosome complex or similar)
Total for Both: 16 proteins/features

In summary:
Prokaryotic cells have mechanisms involving 32 distinct proteins.
Eukaryotic cells utilize mechanisms with 47 distinct proteins.
Shared between both are mechanisms involving 16 distinct proteins or features.

Overall, there are a total of 95 distinct proteins or features involved in error detection during translation across both prokaryotic and eukaryotic cells.

Prokaryotic-Exclusive Mechanisms:

Overview of the quality control, error-check, repair, discard, and recycling mechanisms during prokaryotic translation.

1. Ribosome Stalling and Rescue
Key Players: tmRNA, SmpB, ArfA, ArfB

2. Proteolytic Systems for Truncated Peptides
Key Players: Lon Protease, ClpXP Protease

3. RNA Quality Control for Faulty mRNAs
Key Players: RNase R, PNPase, RNase II

4. Translation Error-Check and Repair
Key Players: EF-Tu, RelA, SpoT

5. Ribosome Collision and Quality Control
Key Players: HflX, RsfA

6. Other Quality Control and Regulatory Factors
Key Players: RqcH, RqcP, YbeY, MazEF

7. Chaperones for Folding and Protein Quality
Key Players: DnaK/DnaJ/GrpE, GroEL/GroES

8. tmRNA-Mediated Ribosome Rescue
Key Players: tmRNA, SmpB

9. Trans-Translation
Key Players: tmRNA, SmpB

10. Lon and Clp Proteases
Key Players: Lon protease, ClpXP, ClpAP

Prokaryotic cells: 10 distinct mechanisms

Eukaryotic-Exclusive Mechanisms:

Overview of the quality control, error-check, repair, discard, and recycling mechanisms in protein synthesis in eukaryotes.

1. Nonsense-Mediated Decay (NMD)
Key Players: UPF1, UPF2, UPF3, SMG1-7

2. No-Go Decay (NGD)
Key Players: Dom34, Hbs1

3. Non-Stop Decay (NSD)
Key Players: Ski7, Hbs1, Pelota

4. Ribosome-Associated Quality Control (RQC)
Key Players: LTN1, NEMF, TCF25

5. mRNA Surveillance
Key Players: eIF4A3, MAGOH, Y14, MLN51

6. Endoplasmic Reticulum (ER)-Associated Degradation (ERAD)
Key Players: EDEM, HERP, SEL1L, HRD1

7. Chaperone-Assisted Protein Quality Control
Key Players: HSP70, HSP90, CHIP

8. Polysome Surveillance
Description: Ensures efficient functioning of polysomes.

9. Translation Fidelity Checkpoints
Description: Ensures accurate decoding of mRNA sequences.

10. Ribosome Function Monitoring
Description: Monitors accurate tRNA to mRNA codon matching.

Eukaryotic cells: 10 distinct mechanisms

Shared Error Detection Mechanisms in Prokaryotic and Eukaryotic Cells:

1. Chaperone-assisted protein quality control:
Prokaryotes: DnaK, DnaJ, GrpE, GroEL, GroES
Eukaryotes: HSP70, HSP90, BiP

2. Proteolytic systems
Prokaryotes: Lon protease, ClpXP protease
Eukaryotes: 26S proteasome system

3. Ribosome stalling and rescue
Prokaryotes: tmRNA, SmpB, ArfA, ArfB
Eukaryotes: Dom34, Hbs1

4. RNA quality control
Prokaryotes: RNase R, PNPase, RNase II
Eukaryotes: Exosome complex, Xrn1

5. Translation fidelity checkpoints
Prokaryotes: EF-Tu
Eukaryotes: eEF1A, aminoacyl-tRNA synthetases

Shared between both: 5 distinct mechanisms

In summary:
Prokaryotic cells: 10 distinct mechanisms
Eukaryotic cells: 10 distinct mechanisms
Shared between both: 5 distinct mechanisms
Overall, there are a total of 25 distinct mechanisms mentioned.

https://reasonandscience.catsboard.com

321Perguntas .... - Page 13 Empty Re: Perguntas .... Thu Oct 26, 2023 6:20 pm

Otangelo


Admin

/ rewrite in bbcode, just focussing exclusively on quality monitoring, error check, repair, discard, and recycle proteins and mechanisms.

Shared Error Detection Mechanisms during Translation in Prokaryotic and Eukaryotic Cells

1. Chaperone-assisted protein quality control:
Prokaryotes (specifically, bacteria):
Proteins: DnaK, DnaJ, GrpE (HSP70 system), GroEL, GroES
Pathway: Chaperones recognize and bind to unfolded proteins, aiding in their refolding.

Eukaryotes:
Proteins: HSP70, HSP90, BiP
Pathway: Chaperone-mediated refolding. Co-chaperones like CHIP tag misfolded proteins for degradation.

2. Proteolytic systems
Prokaryotes:
Proteins: Lon protease, ClpXP protease
Pathway: Degradation of misfolded or damaged proteins.

Eukaryotes:
Proteins: The 26S proteasome system
Pathway: Misfolded proteins are tagged by ubiquitin and degraded by the 26S proteasome.

3. Ribosome stalling and rescue
Prokaryotes:
Proteins: tmRNA, SmpB, ArfA, ArfB
Pathway: tmRNA-SmpB rescues stalled ribosomes.

Eukaryotes:
Proteins: Dom34, Hbs1
Pathway: Dom34 and Hbs1 recognize stalled ribosomes, leading to mRNA cleavage.

4. RNA quality control
Prokaryotes:
Proteins: RNase R, PNPase, RNase II
Pathway: Degradation of faulty mRNA molecules.

Eukaryotes:
Proteins: The exosome complex, Xrn1
Pathway: Degradation of aberrant mRNA molecules.

5. Translation fidelity checkpoints
Prokaryotes:
Proteins: EF-Tu
Pathway: EF-Tu ensures accurate aminoacyl-tRNA delivery.

Eukaryotes:
Proteins: eEF1A, aminoacyl-tRNA synthetases
Pathway: eEF1A ensures proper aminoacyl-tRNA delivery, and synthetases ensure correct amino acid-tRNA charging.

https://reasonandscience.catsboard.com

Otangelo


Admin

Error Check and Repair During Eukaryotic Ribosome Biogenesis and Maturation

Overview
1. rRNA Synthesis: The synthesis of ribosomal RNA (rRNA) is initiated in the nucleolus. RNA polymerase I transcribes a long precursor rRNA, which will give rise to the mature 18S, 5.8S, and 28S rRNAs. 
2. tRNA Processing: tRNAs are transcribed as precursors by RNA polymerase III in the nucleus. These precursors undergo several maturation steps. 
3. rRNA Modification: The precursor rRNA undergoes various modifications facilitated by snoRNPs. 
4. Ribosomal Protein Synthesis: Ribosomal proteins are synthesized in the cytoplasm and then imported into the nucleus for assembly. 
5. Small Subunit (40S in eukaryotes) Assembly: The assembly process involves multiple maturation factors and chaperones. 
6. Large Subunit (60S in eukaryotes) Assembly: The 5.8S, 28S, and 5S rRNAs assemble to form the large subunit with numerous maturation factors. 
7. 80S Ribosome Assembly: The small and large subunits are exported from the nucleolus to the cytoplasm, where they form the functional 80S ribosome. 
8. Quality Control and Recycling: Several mechanisms ensure that only fully assembled ribosomes participate in translation. 
9. Ribosome Function: The fully assembled 80S ribosome facilitates the translation of mRNA into proteins. 
10. Regulation of Ribosome Biogenesis: The production of ribosomes is tightly regulated in response to cellular conditions. 

1. rRNA Synthesis and Initial Processing: Quality Control Mechanisms

Ensuring the fidelity of rRNA modifications is critical for cellular integrity. Eukaryotic cells have developed intricate mechanisms to oversee the synthesis, modification, and processing of rRNAs, ensuring that only correctly modified rRNAs are integrated into ribosomes.

Error Checking:
Nucleolar surveillance: Monitors the nucleolus, targeting improperly modified rRNAs for degradation.
TRAMP complex (in eukaryotes): Flags incorrectly processed and modified rRNAs for degradation by the exosome.

Repair Mechanisms:
The cell employs specific mechanisms such as isomerases for rectifying incorrect modifications and demethylases to remove inappropriate methyl groups. Non-reparable rRNAs are targeted for degradation.

Discard and Recycling Mechanisms:
Exosome (in eukaryotes): Degrades misprocessed or improperly modified rRNAs.
Proteasome (in eukaryotes): Degrades ribosomal proteins associated with flawed rRNAs.
Rrp6 (in eukaryotes): Works alongside the exosome to degrade rRNAs.

rRNA Recycling:
Defective rRNAs are broken down, and their components are recycled. The exosome, especially Rrp6, plays a central role in ensuring efficient recycling of rRNA components.

These mechanisms ensure eukaryotic cells produce functional ribosomes and maintain the quality of protein synthesis, vital for cellular health and function.




2. tRNA Processing

Ensuring the precision and reliability of tRNA molecules is pivotal for accurate protein synthesis and overall cellular function. The synthesis and subsequent processing of tRNA in eukaryotic cells utilize intricate surveillance, modification, degradation, and recycling pathways. These systems ensure that only tRNAs that are correctly processed and modified are recruited for translation.

Error Checking:
Aminoacyl-tRNA synthetases (AARSs): These enzymes are integral to the "proofreading" process, attaching the right amino acid to its corresponding tRNA. Some AARSs possess editing sites to remove incorrectly attached amino acids.
tRNA modification enzymes: These enzymes guarantee the correct modification of specific nucleotides within tRNA molecules. Such modifications can significantly influence translation accuracy.

Repair Mechanisms:
tRNA nucleotidyltransferases: These enzymes add nucleotides to the 3' ends of truncated tRNAs, repairing them.
tRNA ligases: These enzymes mend tRNAs cleaved in the anticodon loop, restoring their function.

Discard and Degradation Mechanisms:
Nuclear surveillance: In eukaryotes, this system rapidly degrades tRNA transcripts that are misprocessed or prematurely terminated within the nucleus.
Cytoplasmic surveillance: It identifies and degrades tRNAs that are either improperly processed, misfolded, or not correctly aminoacylated.
Rrp44/Dis3 and the TRAMP complex: They collaborate to identify and degrade malfunctioning tRNAs in eukaryotic cells.
RTD (Rapid tRNA Decay) pathway: This pathway is responsible for detecting and degrading tRNAs harboring mutations, ensuring they don't enter the translation process.

tRNA Recycling:
The degradation mechanisms breakdown malfunctioning tRNAs into their constituent nucleotides. These can then be recycled within the cellular milieu. Key players in this recycling process include the TRAMP complex and the exosome, ensuring that tRNA components are reutilized efficiently, reducing cellular wastage.

By orchestrating these intricate surveillance, repair, and degradation systems, eukaryotic cells ensure the fidelity of tRNAs. This, in turn, guarantees accurate and efficient protein synthesis, which is indispensable for cell survival and optimal function.

3. rRNA Modification in Eukaryotes

Surveillance Mechanisms in the Nucleolus:
The nucleolus, an intricate region within the eukaryotic cell nucleus, serves as the epicenter for ribosome biogenesis. Throughout this complex process, pre-rRNAs undergo comprehensive processing, intricate modifications, and assembly alongside ribosomal proteins. The cell enforces stringent surveillance mechanisms in the nucleolus to ensure that only correctly processed and assembled ribosomal units proceed to the later stages of ribosome maturation. Any flawed rRNAs or ribonucleoprotein complexes are swiftly recognized and subjected to degradation.

Exosome complex:
A critical multi-protein assembly that orchestrates the 3' to 5' degradation of RNA in eukaryotes.
Primary Function: It targets improperly processed and aberrant rRNA precursors for degradation, ensuring the fidelity of ribosome biogenesis.
Key Components:
RRP6/EXOSC10: An integral ribonuclease of the exosome complex that is particularly active within the nucleolus.
Dis3: Another pivotal ribonuclease within the exosome complex.
Core exosome constituents: A collection of proteins, notable among which are Csl4, Rrp4, and Rrp40.

DOM34-Hbs1 complex:
Functionally and structurally reminiscent of the eukaryotic release factors.
Primary Function: Specializes in detecting and earmarking stalled 60S preribosomes for targeted degradation.

UTP-A, UTP-B, and UTP-C subcomplexes:
These are integral components of the small subunit (SSU) processome in eukaryotic cells.
Primary Function: They contribute to the early processing stages of the 18S rRNA. Abnormalities in these complexes can lead to the accumulation of defective 18S precursors.

Nop53:
Distinguished as a factor in ribosome biogenesis.
Primary Function: Crucial for directing the exosome to preribosomes, marking malfunctioning 60S subunits for degradation.

Mtr4:
This RNA helicase is intrinsic to the eukaryotic degradation machinery.
Primary Function: Facilitates the exosome in degrading misprocessed rRNAs.

Rrp5:
Identified as a multifunctional ribosome biogenesis factor.
Primary Function: Participates in the processing of both the 18S and 25S rRNAs. In instances of binding to aberrant rRNAs, it signals these molecules for degradation.

Together, these molecular watchdogs ensure the utmost fidelity in ribosome biogenesis by eliminating rRNA molecules that are misprocessed, incorrectly modified, or improperly assembled, thereby preventing their incorporation into functional ribosomes.


4. Ribosomal Protein Synthesis in Eukaryotes

Quality Control and Surveillance:
Given the pivotal role of ribosomal proteins (RPs) in orchestrating precise and efficient protein synthesis within eukaryotic cells, there are specialized mechanisms designed to monitor and rectify any discrepancies arising during RP synthesis and assembly.

Ubiquitin-Proteasome System (UPS): This system identifies and marks unassembled or aberrantly folded ribosomal proteins for degradation within the eukaryotic cytoplasm.
ASC1 Complex: Operates within the eukaryotic nucleus to detect and rectify defects in ribosomal protein synthesis and assembly. It ensures that only properly assembled ribosomal subunits make their way to the cytoplasm.

Stabilization Mechanisms:
Although RPs in eukaryotes lack direct repair mechanisms akin to nucleic acids, the cell facilitates their appropriate folding and stabilization with specialized proteins termed molecular chaperones.

Molecular Chaperones: These proteins are pivotal in guiding the proper folding and stabilization of ribosomal proteins within eukaryotic cells. They can assist in refolding proteins that might have initially misfolded.

Elimination Mechanisms:
In eukaryotic cells, ribosomal proteins that don't find their place within ribosomes or are misfolded are swiftly identified and directed towards degradation pathways. This preemptive action curtails their accumulation and potential detrimental consequences.

Proteasome: Within the cytoplasm, ribosomal proteins failing to integrate properly into ribosomes are marked with ubiquitin and channeled for degradation by the proteasome.
Ltn1 E3 Ligase: Engages in targeting nascent ribosomal proteins that misfold during their synthesis, earmarking them for degradation.

Resource Reutilization Mechanisms:
While the ribosomal proteins themselves are not recycled, the amino acids retrieved from their degradation are salvaged and repurposed for synthesizing new proteins within eukaryotic cells.

By leveraging these intricate systems, eukaryotic cells ensure the highest fidelity in ribosomal protein synthesis. Any deviations or errors are promptly addressed. This rigorous oversight is vital for preserving the structural and functional integrity of ribosomes, which, in turn, underpins the overall proteome stability of the cell.


5. Formation of the Small Ribosomal Subunit in Eukaryotes

The construction of the small ribosomal subunit (SSU) within eukaryotic cells unfolds through a series of orchestrated events. It's pivotal to maintain the integrity of SSU assembly, and cells have evolved intricate strategies to pinpoint and rectify discrepancies during this process.

UTP-A, UTP-B, and UTP-C subcomplexes: As integral constituents of the SSU processome in eukaryotes, these subcomplexes drive the primary processing stages of the 18S rRNA. Disruptions or mutations within these components may culminate in the buildup of flawed 18S precursors, thereby activating cellular surveillance pathways.
Nucleolar Quality Control (NoQC): This mechanism zeroes in on malassembled SSU units, earmarking them for degradation and hindering their migration from the nucleolus to the nucleoplasm.

Remediation Strategies:
Direct mending of malassembled SSUs presents a daunting challenge. Eukaryotic cells generally lean towards disassembling and degrading these faulty units, followed by instigating a fresh assembly cycle.

Elimination Protocols:
Any small subunit derivatives or intermediates displaying assembly defects are swiftly identified and channeled towards degradation pathways. This ensures that only SSUs meeting assembly criteria partake in protein synthesis.

Exosome complex: Acting as the frontline RNA catabolic machinery, the exosome complex is primed to degrade rRNA molecules from the small subunit that display processing or assembly irregularities.
DOM34-Hbs1: With a structural and functional semblance to eukaryotic release factors, this duo targets SSU preribosomes caught in assembly stalls, setting them up for degradation.

Reutilization Pathways:
Molecules and components retrieved from dismantled SSU intermediates, encompassing ribosomal proteins and assorted assembly co-factors, are channeled back into successive SSU assembly cycles.

Molecular Chaperones: These custodians facilitate the refolding and recycling of ribosomal proteins, ensuring their apt integration in upcoming SSU assembly endeavors.

The synergistic interplay between these oversight, elimination, and recycling pathways guarantees the flawless assembly of the eukaryotic small ribosomal subunit, which is foundational for protein synthesis initiation. Disruptions or anomalies in its formation can reverberate throughout the cell, potentially compromising proteome quality and cellular vitality.

https://reasonandscience.catsboard.com

323Perguntas .... - Page 13 Empty Re: Perguntas .... Fri Dec 01, 2023 5:53 pm

Otangelo


Admin

Title:
"Unveiling the 3D Mysteries of the Shroud of Turin"
Imagery:
Use a high-resolution, clear image of the Shroud of Turin and the hologram of the face.
Place the image of the Shroud on one side and the hologram on the opposite side for visual balance.
Consider adding a semi-transparent overlay of the hologram onto the Shroud's face to show the congruence.
Content Layout:
Organize the content into distinct sections with clear headings.
Use a column layout to separate historical findings from scientific advancements.
Historical Analysis Section:
Heading: "Historical Enigma"
Summarize the study by Professor Paul Vignon and the observations made.
Use bullet points to list the key qualities that are important for 3D investigations.
Scientific Findings Section:
Heading: "Scientific Breakthroughs"
Detail the confirmation of 3D information by Drs. Jackson and Jumper and Prof. Tamburelli.
Highlight the contributions by Prof. Peter Soons in bullet points.
Holography Innovation Section:
Heading: "Holography and the Shroud"
Describe Dr. Dennis Gabor's invention of holography and Dr. Theodore Maiman's development of the laser.
Include images of the Nobel Prizes or symbols representing the honor.
Typography:
Use modern, readable fonts for text.
Differentiate headings with a larger or bold font.
Consider color-coding the headings to differentiate sections.
Color Scheme:
Use a muted color palette to not detract from the Shroud's image.
Apply color accents to headings and key phrases.
Infographic Footer:
Add a section crediting the original researchers and any sources.
Include a date for when the infographic was created.
Consistency:
Ensure all elements adhere to a grid for a clean, organized look.
Keep iconography and bullet points stylistically consistent.
Interactivity (If Digital):
If the infographic will be presented in a digital format, consider adding interactive elements such as clickable sections that expand with more information.
Quality:
Ensure high-quality printing or digital resolution to maintain the integrity of images and text.
By following this guide, you can create a more engaging and visually appealing infographic that effectively communicates the rich history and scientific analysis of the Shroud of Turin.

https://reasonandscience.catsboard.com

324Perguntas .... - Page 13 Empty Re: Perguntas .... Wed Dec 20, 2023 3:51 pm

Otangelo


Admin

Informationen zur Ausstellung


Perguntas .... - Page 13 Csm_Unbenannt_c9312e9bf2
„Wer ist der Mann auf dem Tuch?“, fragt die erste in Deutschland präsentierte Ausstellung zum Turiner Grabtuch.  
Das Tuch ist ein 4,40 Meter langes und 1,13 Meter breites Leinentuch mit einem angenähten Saum. Es ist ein kostbares Tuch, in einem aufwändigen Fischgrät-Muster gewebt. Auf dem Tuch sieht man in voller Länge das Abbild eines Mannes in Vorder- und Rückansicht.
Bis heute gibt es nur Theorien darüber, wie es entstanden ist.
Unter dem Titel „Wer ist der Mann auf dem Tuch? – Eine Spurensuche" stellt die Ausstellung sowohl wissenschaftliche Forschung wie theologische Sichtweisen zu dem Leinentuch vor.  
Die Ausstellung dokumentiert die Geschichte des Tuches, die naturwissenschaftlichen Erkenntnisse um Wunden und Echtheit - versehen mit biblischen Bezügen und die einmalige Gelegenheit Religion und Wissenschaft erfahrbar zu machen.
Kernstücke der Ausstellung, sind eine originalgetreue Nachbildung des Tuchs sowie eines Korpus', der aus einer 3D-Betrachtung der Spuren am Tuch gefertigt wurde. Aber auch weitere Ausstellungsstücke wie die Dornenhaube und die Nägel, die zur damaligen Zeit bei einer Kreuzigung verwendet wurden, bieten Anregung zur Diskussion. Die Sammlung umfasst 22 Informationsstellen und sieben Vitrinen.
Entwickelt wurde die Ausstellung von den Maltesern und mit Hilfe privater Unterstützer. Die Wanderausstellung ist deutschlandweit zu sehen. Ab 2020 wandert eine weitere Ausstellung durch Südamerika.

https://reasonandscience.catsboard.com

325Perguntas .... - Page 13 Empty Re: Perguntas .... Tue Jan 30, 2024 3:41 am

Otangelo


Admin

Reflection on the Value of Humanity in Christianity
عیسائیت میں انسانیت کی قدر پر عکاسی۔

**English:** If Christianity is true, then we are of infinite value. Even if we are poor sinners, Christ, the alpha and omega, the author of all life, the one that laid the foundations of the earth, which made Adam and Eve from the mud on the earth, became man.  
**Urdu:** اگر عیسائیت سچ ہے، تو ہماری لامحدود قدر ہے۔ اگرچہ ہم غریب گناہگار ہیں، مسیح، ابتدا و انتہا، تمام زندگی کے مصنف، زمین کی بنیاد رکھنے والے، جس نے زمین کی مٹی سے آدم اور حوا کو بنایا، انسان بن گیا۔

**English:** Became one of us. A tiny speck in the universe. He walked among us and showed us his sublime unequaled character. His wonderful, humble being, but brilliant and wise like no man has ever seen.  
**Urdu:** ہم میں سے ایک بن گیا۔ کائنات میں ایک چھوٹی سی دھول۔ اس نے ہمارے درمیان چل کر ہمیں اپنا بے نظیر عظیم کردار دکھایا۔ اس کی شاندار، عاجزی والی ہستی، لیکن کوئی بھی انسان نے کبھی نہیں دیکھی، ایسی روشن اور دانا۔

**English:** He sacrificed Himself, left his unfathomable glory in the presence of the father and holy spirit, to show us who he is. He gave His life so that we could live, and be part of His family.  
**Urdu:** اس نے اپنی قربانی دی، اپنی لازوال شان کو باپ اور روح القدس کی موجودگی میں چھوڑ دیا، تاکہ ہمیں دکھا سکے کہ وہ کون ہے۔ اس نے اپنی زندگی دی تاکہ ہم زندہ رہ سکیں، اور اس کے خاندان کا حصہ بن سکیں۔

**English:** Never, a greater story has been told, and if it's true, which is what I believe, those that belong to Christ, are the most fortunate, and eternity belongs to them. We have value, and we are beloved.  
**Urdu:** کبھی بھی ایک بڑی کہانی نہیں سنائی گئی، اور اگر یہ سچ ہے، جو کہ میں مانتا ہوں، جو مسیح کے ہیں، وہ سب سے زیادہ خوش قسمت ہیں، اور ابدیت ان کی ہے۔ ہماری قدر ہے، اور ہم محبوب ہیں۔

**English:** There is a good reason, why the Gospel is called the good news.  
**Urdu:** اچھی وج

ہ ہے، کہ انجیل کو خوشخبری کہا جاتا ہے۔

Following are Scriptural References on Redemption
فدیہ پر صحیفائی حوالہ جات درج ذیل ہیں۔

**English:** For you were BOUGHT at a price; therefore glorify God in your body and in your spirit, which are God's. - 1 Corinthians 6:20  
**Urdu:** کیونکہ تم ایک قیمت پر خریدے گئے تھے؛ اس لئے اپنے جسم اور اپنی روح میں، جو خدا کی ہیں، خدا کی تمجید کرو۔ - 1 کرنتھیوں 6:20

**English:** Therefore take heed to yourselves and to all the flock, among which the Holy Spirit has made you overseers, to shepherd the church of God which He PURCHASED with His own blood. - Acts 20:28  
**Urdu:** اس لئے خود کو اور سب گلہ کو سنبھالو، جن میں روح القدس نے تمہیں نگہبان بنایا ہے، خدا کی کلیسیا کی رہنمائی کرو، جسے اس نے اپنے خون سے خریدا۔ - اعمال 20:28

**English:** "...just as the Son of Man did not come to be served, but to serve, and to give His life a RANSOM for many." - Matthew 20:28  
**Urdu:** "...جیسا کہ ابن آدم آیا نہیں کہ اس کی خدمت کی جائے بلکہ خدمت کرے، اور اپنی زندگی بہتوں کے لئے فدیہ دے۔" - متی 20:28

**English:** For there is one God and one Mediator between God and men, the Man Christ Jesus, who gave Himself a RANSOM for all, to be testified in due time, - 1 Timothy 2:5-6  
**Urdu:** کیونکہ ایک ہی خدا ہے اور خدا اور انسانوں کے درمیان ایک ہی دلال ہے، وہ انسان مسیح یسوع، جس نے اپنے آپ کو سب کے لئے فدیہ دیا، جس کی بروقت گواہی دی جائے گی، - 1 تیمتھیس 2:5-6

**English:** Knowing that you were not REDEEMED with corruptible things, like silver or gold, from your aimless conduct received by tradition from your fathers, but with the precious blood of Christ, as of a lamb without blemish and without spot. - 1 Peter 1:18-19  
**Urdu:** جان کر کہ تمہیں چاندی یا سونے جیسی فانی چیزوں سے نہیں چھڑایا گیا، جو تمہارے باپ دادا سے موصول ہونے والے بے مقصد طرز عمل سے ہے، بلکہ مسیح کے قیمتی خون سے، جیسے ایک بے عیب اور بے داغ کے برّے کے ساتھ۔ - 1 پطرس 1:18-19


**English:** Christianity offers a unique narrative within the vast mosaic of world religions, characterized by the profound event of the incarnation.  
**Urdu:** عیسائیت دنیا کے مذاہب کے وسیع موزیک میں ایک منفرد کہانی پیش کرتی ہے، جو جسمانیت کے گہرے واقعے سے متصف ہے۔

**English:** In this divine mystery, God chooses to enter our world as Jesus Christ, fully embodying both the divine and the human.  
**Urdu:** اس الہی راز میں، خدا ہماری دنیا میں یسوع مسیح کے طور پر داخل ہونے کا انتخاب کرتا ہے، مکمل طور پر دیوتا اور انسانیت دونوں کو جسمانی شکل دیتا ہے۔

**English:** This act of incarnation is not merely a historical event but a testament to God's deep desire to connect with humanity on a personal level.  
**Urdu:** یہ جسمانیت کا عمل صرف ایک تاریخی واقعہ نہیں بلکہ خدا کی انسانیت سے ذاتی سطح پر جڑنے کی گہری خواہش کی گواہی ہے۔

**English:** Through Jesus' life, we witness the unfolding of divine love in action, engaging with the joys, sorrows, and hopes of human existence.  
**Urdu:** یسوع کی زندگی کے ذریعے، ہم عمل میں الہی محبت کے انکشاف کو دیکھتے ہیں، انسانی وجود کی خوشیوں، غموں، اور امیدوں کے ساتھ مصروف ہوتے ہیں۔

**English:** The climax of this narrative is found in the sacrificial death of Jesus on the cross, an act of redemption that echoes through time.  
**Urdu:** اس کہانی کا عروج صلیب پر یسوع کی قربانی کی موت میں ملتا ہے، ایک نجات دہندہ عمل جو وقت کے ساتھ گونجتا ہے۔

**English:** This pivotal moment transcends a mere historical event; it represents the ultimate expression of divine love, a willing sacrifice for the redemption of humanity.  
**Urdu:** یہ فیصلہ کن لمحہ صرف ایک تاریخی واقعہ سے بڑھ کر ہے؛ یہ الہی محبت کی انتہائی تعبیر کو ظاہر کرتا ہے، انسانیت کی نجات کے لئے ایک رضاکارانہ قربانی۔

**English:** In the face of such profound sacrifice, we are introduced to the concept of grace, a cornerstone of Christian faith.  
**Urdu:** ایسی گہ

ری قربانی کے سامنے، ہمیں فضل کے تصور سے متعارف کرایا جاتا ہے، جو عیسائی ایمان کا ایک بنیادی پتھر ہے۔

**English:** Grace is the unmerited favor from God, a gift that is not earned but generously given, embodying God's merciful nature.  
**Urdu:** فضل خدا کی طرف سے غیر مستحق مہربانی ہے، ایک تحفہ جو کمایا نہیں جاتا بلکہ بخشش سے دیا جاتا ہے، جو خدا کی رحم دل فطرت کو ظاہر کرتا ہے۔

**English:** This grace invites us into a relationship with God that is based on faith and trust, rather than our own merits or efforts.  
**Urdu:** یہ فضل ہمیں خدا کے ساتھ ایک تعلق میں دعوت دیتا ہے جو ایمان اور اعتماد پر مبنی ہوتا ہے، بجائے ہماری اپنی حق داریوں یا کوششوں کے۔

**English:** In the broader context of world religions, many traditions emphasize the attainment of divine favor through human actions and piety.  
**Urdu:** عالمی مذاہب کے وسیع تناظر میں، بہت سی روایات انسانی عملوں اور تقویٰ کے ذریعے الہی مہربانی حاصل کرنے پر زور دیتی ہیں۔

**English:** However, Christianity diverges significantly in this regard, presenting a path of salvation that is anchored in the grace and mercy of God.  
**Urdu:** تاہم، عیسائیت اس سلسلے میں بہت مختلف ہے، نجات کا ایک راستہ پیش کرتی ہے جو خدا کے فضل اور رحم پر مبنی ہے۔

**English:** The Christian journey is thus not one of earning salvation through deeds but of accepting the gift of grace through faith in Jesus Christ.  
**Urdu:** اس طرح عیسائی سفر اعمال کے ذریعے نجات حاصل کرنے کا نہیں بلکہ یسوع مسیح میں ایمان کے ذریعے فضل کے تحفے کو قبول کرنے کا ہے۔

**English:** This transformative power of grace leads to a life of spiritual renewal and moral improvement, not as a means to salvation but as a response to God's love.  
**Urdu:** فضل کی اس تبدیلی کی طاقت روحانی تجدید اور اخلاقی بہتری کی زندگی کی طرف لے جاتی ہے، نجات حاصل کرنے کے ذرائع کے طور پر نہیں بلکہ خدا کی محبت کے جواب کے طور پر۔

**English:** In embracing this narrative, we find a message of hope and redemption, a call to experience the depth of God's love and the transformative power of His grace.  
**Urdu:**اس داستان کو اپنانے میں، ہمیں امید اور نجات کا پیغام ملتا ہے، خدا کی محبت کی گہرائی اور اس کے فضل کی تبدیلی کی طاقت کا تجربہ کرنے کی دعوت۔

https://reasonandscience.catsboard.com

Sponsored content



Back to top  Message [Page 13 of 14]

Go to page : Previous  1 ... 8 ... 12, 13, 14  Next

Permissions in this forum:
You cannot reply to topics in this forum