GroES binding regulates GroEL chaperonin activity under heat shock.

Details

Serval ID
serval:BIB_7167E4FC2CFD
Type
Article: article from journal or magazin.
Collection
Publications
Title
GroES binding regulates GroEL chaperonin activity under heat shock.
Journal
FEBS Letters
Author(s)
Goloubinoff P., Diamant S., Weiss C., Azem A.
ISSN
0014-5793 (Print)
ISSN-L
0014-5793
Publication state
Published
Issued date
1997
Volume
407
Number
2
Pages
215-219
Language
english
Abstract
Chaperonins GroEL14 and GroES7 are heat-shock proteins implicated in the molecular response to stress. Protein fluorescence, crosslinking and kinetic analysis revealed that the bond between the two otherwise thermoresistant oligomers is regulated by temperature. As temperature increased, the affinity of GroES7 and the release of bound proteins from the chaperonin concomitantly decreased. After heat shock, GroES7 rebinding to GroEL14 and GroEL14GroES7 particles correlated with the restoration of optimal protein folding/release activity. Chaperonins thus behave as a molecular thermometer which can inhibit the release of aggregation-prone proteins during heat shock and restore protein folding and release after heat shock.
Keywords
Adenosine Triphosphatases/metabolism, Chaperonin 10/metabolism, Chaperonin 60/metabolism, Cross-Linking Reagents, Heat-Shock Response, L-Lactate Dehydrogenase/metabolism, Malate Dehydrogenase/metabolism, Protein Binding, Protein Denaturation, Protein Folding, Temperature
Pubmed
Web of science
Create date
24/01/2008 20:02
Last modification date
20/08/2019 14:29
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