The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

J Martin; M Mayhew; T Langer; F U Hartl

doi:10.1038/366228a0

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

Nature. 1993 Nov 18;366(6452):228-33. doi: 10.1038/366228a0.

Authors

J Martin¹, M Mayhew, T Langer, F U Hartl

Affiliation

¹ Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

PMID: 7901770
DOI: 10.1038/366228a0

Abstract

The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Diphosphate / metabolism
Adenosine Triphosphate / metabolism
Bacterial Proteins / metabolism*
Chaperonin 10
Chaperonin 60
Cross-Linking Reagents
Escherichia coli / metabolism
Heat-Shock Proteins / metabolism*
Models, Biological
Nucleotides / metabolism
Protein Binding
Protein Folding*
Succinimides

Substances

Bacterial Proteins
Chaperonin 10
Chaperonin 60
Cross-Linking Reagents
Heat-Shock Proteins
Nucleotides
Succinimides
N-succinimidyl 3-(2-pyridyldithio)propionate
Adenosine Diphosphate
Adenosine Triphosphate