Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones.

Détails

ID Serval
serval:BIB_85CE7270F7F4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones.
Périodique
Journal of Biological Chemistry
Auteur(s)
Ben-Zvi A., De Los Rios P., Dietler G., Goloubinoff P.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
2004
Peer-reviewed
Oui
Volume
279
Numéro
36
Pages
37298-37303
Langue
anglais
Résumé
Hsp70 is a central molecular chaperone that passively prevents protein aggregation and uses the energy of ATP hydrolysis to solubilize, translocate, and mediate the proper refolding of proteins in the cell. Yet, the molecular mechanism by which the active Hsp70 chaperone functions are achieved remains unclear. Here, we show that the bacterial Hsp70 (DnaK) can actively unfold misfolded structures in aggregated polypeptides, leading to gradual disaggregation. We found that the specific unfolding and disaggregation activities of individual DnaK molecules were optimal for large aggregates but dramatically decreased for small aggregates. The active unfolding of the smallest aggregates, leading to proper global refolding, required the cooperative action of several DnaK molecules per misfolded polypeptide. This finding suggests that the unique ATP-fueled locking/unlocking mechanism of the Hsp70 chaperones can recruit random chaperone motions to locally unfold misfolded structures and gradually disentangle stable aggregates into refoldable proteins.
Mots-clé
Chromatography, Gel, Escherichia coli Proteins/metabolism, HSP70 Heat-Shock Proteins/metabolism, Leuconostoc/metabolism, Protein Binding, Protein Folding, Solubility
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 15:45
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