GroES binding regulates GroEL chaperonin activity under heat shock

被引：37

作者：

Goloubinoff, P

Diamant, S

Weiss, C

Azem, A

机构：

[1] Department of Plant Sciences, Alexander Silberman Inst. of Life S., Hebrew University of Jerusalem

[2] Biozentrum, Universität Basel, CH-4056 Basel

来源：

FEBS LETTERS | 1997年 / 407卷 / 02期

关键词：

GroE chaperone; molecular thermometer; heat shock; protein folding;

D O I：

10.1016/S0014-5793(97)00348-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1997 Federation of European Biochemical Societies.

引用

页码：215 / 219

页数：5

共 35 条

[1] CHARACTERIZATION OF A FUNCTIONAL GROEL(14)(GROES(7))(2) CHAPERONIN HETERO-OLIGOMER [J].