Coupling between protein folding and allostery in the GroE chaperonin system

Ofer Yifrach, Amnon Horovitz

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


GroEL is an allosteric protein that facilitates protein folding in an ATP-dependent manner. Herein, the relationship between cooperative ATP binding by GroEL and the kinetics of GroE-assisted folding of two substrates with different GroES dependence, mouse dihydrofolate reductase (mDHFR) and mitochondrial malate dehydrogenase, is examined by using cooperativity mutants of GroEL. Strong intra-ring positive cooperativity in ATP binding by GroEL decreases the rate of GroEL-assisted mDHFR folding owing to a slow rate of the ATP-induced transition from the protein-acceptor state to the protein- release state. Inter-ring negative cooperativity in ATP binding by GroEL is found to affect the kinetic partitioning of mDHFR, but not of mitochondrial malate dehydrogenase, between folding in solution and folding in the cavity underneath GroES. Our results show that protein folding by this 'two-stroke motor' is coupled to cooperative ATP binding.

Original languageEnglish
Pages (from-to)1521-1524
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number4
StatePublished - 15 Feb 2000
Externally publishedYes

ASJC Scopus subject areas

  • General


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