GroES binding regulates GroEL chaperonin activity under heat shock

Pierre Goloubinoff*, Sophia Diamant, Celeste Weiss, Abdussalam Azem

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)215-219
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - 28 Apr 1997
Externally publishedYes


  • GroE chaperone
  • Heat shock
  • Molecular thermometer
  • Protein folding


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