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Birth, life and death of nascent polypeptide chains

The journey of nascent polypeptides from synthesis at the peptidyl transferase center of the ribosome (“birth”) to full function (“maturity”) involves multiple interactions, constraints, modifications and folding events. Each step of this journey impacts the ultimate expression level and functional...

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Detalles Bibliográficos
Autores principales: Jha, Sujata, Komar, Anton A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130931/
https://www.ncbi.nlm.nih.gov/pubmed/21538896
http://dx.doi.org/10.1002/biot.201000327
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author Jha, Sujata
Komar, Anton A
author_facet Jha, Sujata
Komar, Anton A
author_sort Jha, Sujata
collection PubMed
description The journey of nascent polypeptides from synthesis at the peptidyl transferase center of the ribosome (“birth”) to full function (“maturity”) involves multiple interactions, constraints, modifications and folding events. Each step of this journey impacts the ultimate expression level and functional capacity of the translated protein. It has become clear that the kinetics of protein translation is predominantly modulated by synonymous codon usage along the mRNA, and that this provides an active mechanism for coordinating the synthesis, maturation and folding of nascent polypeptides. Multiple quality control systems ensure that proteins achieve their native, functional form. Unproductive co-translational folding intermediates that arise during protein synthesis may undergo enhanced interaction with components of these systems, such as chaperones, and/or be subjects of co-translational degradation (“death”). This review provides an overview of our current understanding of the complex co-translational events that accompany the synthesis, maturation, folding and degradation of nascent polypeptide chains.
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spelling pubmed-31309312011-07-13 Birth, life and death of nascent polypeptide chains Jha, Sujata Komar, Anton A Biotechnol J Review The journey of nascent polypeptides from synthesis at the peptidyl transferase center of the ribosome (“birth”) to full function (“maturity”) involves multiple interactions, constraints, modifications and folding events. Each step of this journey impacts the ultimate expression level and functional capacity of the translated protein. It has become clear that the kinetics of protein translation is predominantly modulated by synonymous codon usage along the mRNA, and that this provides an active mechanism for coordinating the synthesis, maturation and folding of nascent polypeptides. Multiple quality control systems ensure that proteins achieve their native, functional form. Unproductive co-translational folding intermediates that arise during protein synthesis may undergo enhanced interaction with components of these systems, such as chaperones, and/or be subjects of co-translational degradation (“death”). This review provides an overview of our current understanding of the complex co-translational events that accompany the synthesis, maturation, folding and degradation of nascent polypeptide chains. WILEY-VCH Verlag 2011-06 /pmc/articles/PMC3130931/ /pubmed/21538896 http://dx.doi.org/10.1002/biot.201000327 Text en Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Review
Jha, Sujata
Komar, Anton A
Birth, life and death of nascent polypeptide chains
title Birth, life and death of nascent polypeptide chains
title_full Birth, life and death of nascent polypeptide chains
title_fullStr Birth, life and death of nascent polypeptide chains
title_full_unstemmed Birth, life and death of nascent polypeptide chains
title_short Birth, life and death of nascent polypeptide chains
title_sort birth, life and death of nascent polypeptide chains
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130931/
https://www.ncbi.nlm.nih.gov/pubmed/21538896
http://dx.doi.org/10.1002/biot.201000327
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