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GroES binding regulates GroEL chaperonin activity under heat shock
Author(s) -
Goloubinoff Pierre,
Diamant Sophia,
Weiss Celeste,
Azem Abdussalam
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00348-7
Subject(s) - groes , groel , chaperonin , protein folding , heat shock protein , biophysics , folding (dsp implementation) , shock (circulatory) , chemistry , microbiology and biotechnology , biochemistry , biology , medicine , escherichia coli , electrical engineering , gene , engineering
Chaperonins GroEL 14 and GroES 7 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 GroES 7 and the release of bound proteins from the chaperonin concomitantly decreased. After heat shock, GroES 7 rebinding to GroEL 14 and GroEL 14 GroES 7 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.