Nature and Regulation of Protein Folding on the Ribosome.
co-translational folding
free energy landscape
molecular chaperones
protein synthesis
translation kinetics
Journal
Trends in biochemical sciences
ISSN: 0968-0004
Titre abrégé: Trends Biochem Sci
Pays: England
ID NLM: 7610674
Informations de publication
Date de publication:
11 2019
11 2019
Historique:
received:
19
02
2019
revised:
10
06
2019
accepted:
14
06
2019
pubmed:
16
7
2019
medline:
29
7
2020
entrez:
15
7
2019
Statut:
ppublish
Résumé
Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein synthesis of the free energy landscapes that underlie co-translational folding and discuss the critical coupling between these landscapes and the rate of translation that ultimately determines the success or otherwise of the folding process. Recent developments have revealed a variety of mechanisms by which both folding and translation can be modulated or regulated, and we discuss how these effects are utilised by the cell to optimise the outcome of protein biosynthesis.
Identifiants
pubmed: 31301980
pii: S0968-0004(19)30141-0
doi: 10.1016/j.tibs.2019.06.008
pmc: PMC7471843
pii:
doi:
Substances chimiques
Molecular Chaperones
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
914-926Subventions
Organisme : Wellcome Trust
ID : 206409/Z/17/Z
Pays : United Kingdom
Informations de copyright
Copyright © 2019 The Author(s). Published by Elsevier Ltd.. All rights reserved.
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