Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
- 1 July 1991
- journal article
- Published by Springer Nature in Nature
- Vol. 352 (6330), 36-42
- https://doi.org/10.1038/352036a0
Abstract
Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg-ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.Keywords
This publication has 52 references indexed in Scilit:
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991
- The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellBiochemistry, 1990
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteinsCell, 1989
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988
- Coming in from the coldNature, 1988
- Proteins as molecular chaperonesNature, 1987
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Host participation in bacteriophage lambda head assemblyJournal of Molecular Biology, 1973
- Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE): II. The propagation of phage λJournal of Molecular Biology, 1973