Co-operative binding of hsp60 may promote transfer hsp70 and correct folding of imported proteins in mitochondria

AbstractI 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 and hsp6O promotes corrert folding or the substrate protein while hsp70 does not