Review: allostery in chaperonins.

Abstract:

: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 inter-ring 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.

journal_name

J Struct Biol

authors

Horovitz A,Fridmann Y,Kafri G,Yifrach O

doi

10.1006/jsbi.2001.4377

keywords:

subject

Has Abstract

pub_date

2001-08-01 00:00:00

pages

104-14

issue

2

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(01)94377-1

journal_volume

135

pub_type

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