GroES binding regulates GroEL chaperonin activity under heat shock.

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.

• Authors: P Goloubinoff, S Diamant, C Weiss, A Azem
• Journal: FEBS letters (FEBS Lett) Vol. 407 Issue 2 Pg. 215-9 (Apr 28 1997) ISSN: 0014-5793 [Print] England
• PMID: 9166902 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chaperonin 10
• Chaperonin 60
• Cross-Linking Reagents
• L-Lactate Dehydrogenase
• Malate Dehydrogenase
• Adenosine Triphosphatases

Topics

• 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