Co-operative binding of hsp60 may promote transfer from hsp70 and correct folding of imported proteins in mitochondria [corrected].
I propose that a molecular chaperone hsp60 binds to and dissociates from the unfolded polypeptide or folding intermediate in a positively co-operative manner, but another chaperone hsp70 shows no such co-operativity. This could simply explain the fact that the protein newly imported in the mitochondrial matrix is transferred from hsp70 to hsp60 promotes correct folding of the substrate protein while hsp70 does not.
Endo
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Department of Chemistry, Faculty of Science, Nagoya University, Japan.
D001692:Biological Transport; D018834:Chaperonin 60; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D011487:Protein Conformation
D018834:Chaperonin 60; D006360:Heat-Shock Proteins