GroES binding regulates GroEL chaperonin activity under heat shock

FEBS Letters
P GoloubinoffA Azem

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.

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Citations

May 19, 1998·Trends in Biochemical Sciences·A RichardsonC Georgopoulos
Mar 15, 2001·Proceedings of the National Academy of Sciences of the United States of America·Z TörökL Vigh
Dec 23, 1998·Proceedings of the National Academy of Sciences of the United States of America·A P Ben-ZviP Goloubinoff
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Sep 27, 2015·Toxicological Sciences : an Official Journal of the Society of Toxicology·Qiang ZhangMelvin E Andersen
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