Allostery in chaperonins

Amnon Horovitz, Yael Fridmann, Galit Kafri, Ofer Yifrach

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish
Pages (from-to)115-131
Number of pages17
JournalRendiconti Lincei
Volume17
Issue number1-2
DOIs
StatePublished - 1 Mar 2006
Externally publishedYes

Keywords

  • Chaperonins
  • Cooperativity
  • GroEL
  • Nested allostery
  • Protein machines

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