GroES binding regulates GroEL chaperonin activity under heat shock

FEBS Letters

Azem, Abdussalam¹  Weiss, Celeste¹  Diamant, Sophia¹  Goloubinoff, Pierre¹ 

[1]Department of Plant Sciences, Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, 1904 Jerusalem, Israel

关键词: GroE chaperone;    Molecular thermometer;    Heat shock;    Protein folding;    MDH;    mitochondrial malate dehydrogenase;    LDH;    lactate dehydrogenase;    S:L;    GroES:GroEL molar ratio;    L14;    GroEL14;    S7;    GroES7;   

DOI  :  10.1016/S0014-5793(97)00348-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown