GroES binding regulates GroEL chaperonin activity under heat shock.

Détails

ID Serval
serval:BIB_7167E4FC2CFD
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
GroES binding regulates GroEL chaperonin activity under heat shock.
Périodique
FEBS Letters
Auteur(s)
Goloubinoff P., Diamant S., Weiss C., Azem A.
ISSN
0014-5793 (Print)
ISSN-L
0014-5793
Statut éditorial
Publié
Date de publication
1997
Volume
407
Numéro
2
Pages
215-219
Langue
anglais
Résumé
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.
Mots-clé
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
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 15:29
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