The mechanism of Hsp70 chaperones: (entropic) pulling the models together.

Détails

ID Serval
serval:BIB_C08C34ED707D
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
The mechanism of Hsp70 chaperones: (entropic) pulling the models together.
Périodique
Trends in Biochemical Sciences
Auteur(s)
Goloubinoff P., De Los Rios P.
ISSN
0968-0004[print], 0968-0004[linking]
Statut éditorial
Publié
Date de publication
2007
Volume
32
Numéro
8
Pages
372-380
Langue
anglais
Résumé
Hsp70s are conserved molecular chaperones that can prevent protein aggregation, actively unfold, solubilize aggregates, pull translocating proteins across membranes and remodel native proteins complexes. Disparate mechanisms have been proposed for the various modes of Hsp70 action: passive prevention of aggregation by kinetic partitioning, peptide-bond isomerase, Brownian ratcheting or active power-stroke pulling. Recently, we put forward a unifying mechanism named 'entropic pulling', which proposed that Hsp70 uses the energy of ATP hydrolysis to recruit a force of entropic origin to locally unfold aggregates or pull proteins across membranes. The entropic pulling mechanism reproduces the expected phenomenology that inspired the other disparate mechanisms and is, moreover, simple.
Mots-clé
Adenosine Triphosphate/chemistry, Animals, Binding Sites, Entropy, HSP70 Heat-Shock Proteins/physiology, Humans, Hydrolysis, Kinetics, Models, Molecular, Molecular Chaperones/chemistry, Molecular Chaperones/metabolism, Molecular Conformation, Peptides/chemistry, Protein Conformation, Protein Denaturation, Protein Folding
Pubmed
Web of science
Création de la notice
24/01/2008 20:02
Dernière modification de la notice
20/08/2019 15:35
Données d'usage