Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.
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.
Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, New York 10021.
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D001426:Bacterial Proteins / Q000494:pharmacology*; D018834:Chaperonin 60; D002850:Chromatography, Gel; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000494:pharmacology*; D066298:In Vitro Techniques; D008954:Models, Biological; D011487:Protein Conformation / Q000187:drug effects*; D013884:Thiosulfate Sulfurtransferase / Q000187:drug effects
D001426:Bacterial Proteins; D018834:Chaperonin 60; C494635:DnaJ protein, E coli; D029968:Escherichia coli Proteins; C068113:GrpE protein, Bacteria; C489400:GrpE protein, E coli; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D013884:Thiosulfate Sulfurtransferase; C063842:dnaK protein, E coli