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

Nature. 1992 Apr 23;356(6371):683-9. doi: 10.1038/356683a0.


The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins* / pharmacology*
  • Chaperonin 60
  • Chromatography, Gel
  • Dose-Response Relationship, Drug
  • Escherichia coli
  • Escherichia coli Proteins*
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins*
  • Heat-Shock Proteins* / pharmacology*
  • In Vitro Techniques
  • Models, Biological
  • Protein Conformation / drug effects*
  • Thiosulfate Sulfurtransferase* / drug effects


  • Bacterial Proteins
  • Chaperonin 60
  • DnaJ protein, E coli
  • Escherichia coli Proteins
  • GrpE protein, Bacteria
  • GrpE protein, E coli
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Thiosulfate Sulfurtransferase
  • dnaK protein, E coli