Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.
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.
Horwich
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AL
Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510.
Willison
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KR
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D018834:Chaperonin 60; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D004926:Escherichia coli / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D046911:Macromolecular Substances; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
D001426:Bacterial Proteins; D018834:Chaperonin 60; D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D011506:Proteins; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins