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 Bioljournal_title
Journal of structural biologyauthors
Horovitz A,Fridmann Y,Kafri G,Yifrach Odoi
10.1006/jsbi.2001.4377keywords:
subject
Has Abstractpub_date
2001-08-01 00:00:00pages
104-14issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(01)94377-1journal_volume
135pub_type
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