Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
- 29 March 1993
- journal article
- review article
- Published by The Royal Society in Philosophical Transactions Of The Royal Society B-Biological Sciences
- Vol. 339 (1289) , 313-326
- https://doi.org/10.1098/rstb.1993.0030
Abstract
Two families of molecular chaperone, the hsp 60-GroEL family and the TF55-TCP1 family, have been discovered in evolutionarily related cellular compartments. A member of one of these families, hsp 60, has been shown to play a global role in polypeptide chain folding in mitochondria. We review here studies of both hsp 60 and other family members, discussing their essential physiological roles and mechanism of action.Keywords
This publication has 111 references indexed in Scilit:
- A polypeptide bound by the chaperonin groEL is localized within a central cavity.Proceedings of the National Academy of Sciences, 1993
- Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants.Proceedings of the National Academy of Sciences, 1992
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- GroE facilitates refolding of citrate synthase by suppressing aggregationBiochemistry, 1991
- Mitochondrial proteins essential for viability mediate protein import into yeast mitochondriaNature, 1991
- The mitochondrial chaperonin hsp60 is required for its own assemblyNature, 1990
- Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and AssemblyScience, 1990
- Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondriaNature, 1989
- Gene organization and structure of two transcriptional units from Methanococcus coding for ribosomal proteins and elongation factorsCanadian Journal of Microbiology, 1989
- Transient association of newly synthesized unfolded proteins with the heat-shock GroEL proteinNature, 1988