Kinesis of Polypeptide during GroEL-mediated Folding
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Excerpt
The mechanism by which the large double-ring structures known as chaperonins facilitate the ATP-dependent folding to native form of a large number of newly synthesized and newly translocated polypeptides has been a subject of considerable interest in the general area of protein kinesis. Recent structural and functional studies of the bacterial chaperonin GroEL have begun to inform on this process, in particular conveying information on what happens to the protein substrate during such a reaction. Here we summarize these findings and discuss their implications, and also consider issues that remain unsettled, likely targets of futureexperimentation.
BINDING NONNATIVE POLYPEPTIDES
In vivo experiments with both Hsp60 in yeast mitochondria (Cheng et al. 1989) and GroEL in Escherichia coli (Horwich et al. 1993) show that deficiency of chaperonin function results in wholesale aggregation of imported or newly synthesized proteins, respectively. This suggests that chaperonins bind newly synthesized or translocated proteins before they acquire...
