Review: Allostery in Chaperonins

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 i...

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Bibliographic Details
Published inJournal of Structural Biology Vol. 135; no. 2; pp. 104 - 114
Main Authors Horovitz, Amnon, Fridmann, Yael, Kafri, Galit, Yifrach, Ofer
Format Book Review Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.08.2001
Subjects
Allosteric Regulation - physiology
Animals
chaperonins
Chaperonins - drug effects
cooperativity
GroEL
Humans
Kinetics
Ligands
Models, Chemical
nested allostery
protein machines
Proteins - metabolism
Proteins - pharmacology
chaperonins
cooperativity
GroEL
protein machines
nested allostery
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Summary: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.
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ISSN:1047-8477
1095-8657
DOI:10.1006/jsbi.2001.4377