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

T Langer; C Lu; H Echols; J Flanagan; M K Hayer; F U Hartl

doi:10.1038/356683a0

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.

Authors

T Langer¹, C Lu, H Echols, J Flanagan, M K Hayer, F U Hartl

Affiliation

¹ Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, New York 10021.

PMID: 1349157
DOI: 10.1038/356683a0

Abstract

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

Substances

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