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.
Subject
General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology
Reference132 articles.
1. Cloning of a Chinese hamster protein homologous to the mouse /-complex protein TCP-1: structural similarity to the ubiquitous "chaperonin'' family of heat shock proteins. Biochim. biophys;Ahmad S.;Acta,1990
2. Gene organization and structure of two transcriptional units from Methanococcus coding for ribosomal proteins and elongation factors
3. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
4. Baker K.P. & Schatz G. 1991 Mitochondrial proteins essential for viability mediate protein import into yeast mitochondria. Nature Lond. 349 205-208.
5. Assembly of newlysynthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim. biophys;Barraclough R.;Acta.,1980
Cited by
119 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献