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By Robert L. Ellis

The 1st of its type, this quantity provides the newest learn findings at the chaperonins, the simplest studied relatives of a category of proteins often called molecular chaperones. those findings are altering our view of a few primary mobile tactics concerning proteins, in particular how proteins fold into their sensible conformations. Key positive factors* Origins of the recent view of protein folding* Prokaryotic chaperonins* Eukaryotic chaperonins* Evolution of the chaperonins* Refolding of denatured proteins* Organelle biosynthesis* Biomedical features

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And Lorimer, G. H. (1989). Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and ATP. Nature {London) 342, 884-889. Goodsell, D. S. (1991). Inside a living cell. Trends Biochem. Sci. 16, 203-206. , Gaitanaris, G. , Gottesman, M. , and Nikiforov, V. (1992). Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl. Acad. Sci. USA 89,10,341-10,344. Hallberg, E.

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This Page Intentionally Left Blank 2 Evolutionary Relationships of Chaperonins RADHEY S. GUPTA Department of Biochemistry McMaster University Hamilton, Canada L8N 3Z5 I. Introduction II. Chaperonin 60 and Chaperonin 10 Gene Families A. Sequence Characteristics of Chaperonin 60 and Chaperonin 10 FamiUes B. Sequence Similarity between Chaperonin 10 and Chaperonin 60 C. Sequence Similarity between Chaperonin 60 and Other Proteins D. Phylogenetic Analysis Based on Chaperonin 60 and Chaperonin 10 Sequences III.

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