Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

Thomas Langer, Chi Lu, Harrison Echols, John Flanagan, Manajit K. Hayer, F. Ulrich Hartl

Research output: Contribution to journalArticlepeer-review

756 Scopus citations

Abstract

The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding poly-peptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.

Original languageEnglish (US)
Pages (from-to)683-689
Number of pages7
JournalNature
Volume356
Issue number6371
DOIs
StatePublished - Jan 1 1992

All Science Journal Classification (ASJC) codes

  • General

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