Physiological roles of the DnaK and GroE stress proteins: catalysts of protein folding or macromolecular sponges?
- 1 March 1991
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 5 (3) , 529-534
- https://doi.org/10.1111/j.1365-2958.1991.tb00724.x
Abstract
Summary: When organisms ranging from microbes to man are subjected to certain environmental stresses a characteristic heat shock’ response is observed. In Escherichia coli this response is characterized by the induction of several proteins, three of which are the 70 kilodalton product of the dnaK gene, the 60 kilodalton product of the groEL (mopA) gene and the 15 kilodalton product of the groES (mopB) gene. In this review, utilizing enteric bacteria as model organisms, we focus on the role of these proteins within the context provided by well‐established functions of other heat shock products. These facts serve as a starting point from which to speculate upon the in vivo role of these proteins during steady‐state growth.Keywords
This publication has 31 references indexed in Scilit:
- Renaturation of denatured λ repressor requires heat shock proteinsCell, 1990
- Induction of Salmonella Stress Proteins Upon Infection of MacrophagesScience, 1990
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.Plant Cell, 1989
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Demonstration by genetic suppression of interaction of GroE products with many proteinsNature, 1989
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondriaNature, 1989
- Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress.Genes & Development, 1988
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986