Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations

Itamar Kass, Amnon Horovitz

Research output: Contribution to journalArticlepeer-review

162 Scopus citations


An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5′-triphosphate-induced conformational changes that are reflected in binding of adenosine 5′-triphosphate with positive cooperativity within rings and negative cooperativity between rings. Herein, correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its co-chaperonin GroES. It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES. The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system.

Original languageEnglish
Pages (from-to)611-617
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Issue number4
StatePublished - 1 Sep 2002
Externally publishedYes


  • Chaperonins
  • Cooperativity
  • GroES
  • Molecular chaperones
  • Nested allostery
  • Protein folding

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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