Review: Allostery in chaperonins

被引：92

作者：

Horovitz, A ^{[1
]}

Fridmann, Y ^{[1
]}

Kafri, G ^{[1
]}

Yifrach, O ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2001年 / 135卷 / 02期

基金：

以色列科学基金会;

关键词：

nested allostery; cooperativity; GroEL; chaperonins; protein machines;

D O I：

10.1006/jsbi.2001.4377

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 mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative interring cooperativity in ATP binding. Both types of cooperativity are modulated by various heterotropic allosteric effectors, which include nonfolded proteins, ADP, Mg2+, monovalent ions such as K+, and cochaperonins in the case of type I chaperonins such as GroEL. Here, the allosteric properties of chaperonins are reviewed and new results of ours are presented with regard to allosteric effects of ADP. The role of allostery in the reaction cycle and folding function of chaperonins is discussed. (C) 2001 Academic Press.

引用

页码：104 / 114

页数：11

共 73 条

[1] Inter-ring communication is disrupted in the GroEL mutant Arg13->Gly; Ala126->Val with known crystal structure [J].