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

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Version: Author's accepted manuscript
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State: Public
Version: Supplementary document
Serval ID
serval:BIB_1B1B8E4670A2
Type
Article: article from journal or magazin.
Collection
Publications
Title
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.
Journal
Nature Chemical Biology
Author(s)
Goloubinoff P., Sassi A.S., Fauvet B., Barducci A., De Los Rios P.
ISSN
1552-4469 (Electronic)
ISSN-L
1552-4450
Publication state
Published
Issued date
2018
Peer-reviewed
Oui
Volume
14
Number
4
Pages
388-395
Language
english
Abstract
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.

Keywords
Cell Biology, Molecular Biology
Pubmed
Web of science
Open Access
Yes
Create date
15/03/2018 10:13
Last modification date
20/08/2019 13:51
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