Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.

Détails

Ressource 1Télécharger: Goloubinoff natChemBiol.pdf (957.54 [Ko])
Etat: Public
Version: Author's accepted manuscript
Document(s) secondaire(s)
Télécharger: News&Views.pdf (1351.76 [Ko])
Etat: Public
Version: Supplementary document
ID Serval
serval:BIB_1B1B8E4670A2
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.
Périodique
Nature Chemical Biology
Auteur(s)
Goloubinoff P., Sassi A.S., Fauvet B., Barducci A., De Los Rios P.
ISSN
1552-4469 (Electronic)
ISSN-L
1552-4450
Statut éditorial
Publié
Date de publication
2018
Peer-reviewed
Oui
Volume
14
Numéro
4
Pages
388-395
Langue
anglais
Résumé
During and after protein translation, molecular chaperones require ATP hydrolysis to favor the native folding of their substrates and, under stress, to avoid aggregation and revert misfolding. Why do some chaperones need ATP, and what are the consequences of the energy contributed by the ATPase cycle? Here, we used biochemical assays and physical modeling to show that the bacterial chaperones GroEL (Hsp60) and DnaK (Hsp70) both use part of the energy from ATP hydrolysis to restore the native state of their substrates, even under denaturing conditions in which the native state is thermodynamically unstable. Consistently with thermodynamics, upon exhaustion of ATP, the metastable native chaperone products spontaneously revert to their equilibrium non-native states. In the presence of ATPase chaperones, some proteins may thus behave as open ATP-driven, nonequilibrium systems whose fate is only partially determined by equilibrium thermodynamics.

Mots-clé
Cell Biology, Molecular Biology
Pubmed
Web of science
Open Access
Oui
Création de la notice
15/03/2018 10:13
Dernière modification de la notice
20/08/2019 13:51
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