Review: Allostery in chaperonins

Amnon Horovitz, Yael Fridmann, Galit Kafri, Ofer Yifrach

Research output: Contribution to journalReview articlepeer-review

102 Scopus citations


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)104-114
Number of pages11
JournalJournal of Structural Biology
Issue number2
StatePublished - 1 Jan 2001
Externally publishedYes


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

ASJC Scopus subject areas

  • Structural Biology


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