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••], assessing the effects of trap GroEL expression on growth and protein folding in the budding yeast S. cerevisiae. Again, cell growth is unaffected by trap GroEL and most newly made polypeptides are not detectably bound by the trap; however, mutants of TRiC or its putative co-chaperone GimC do cause many newly made polypeptides to be exposed to the trap. These important findings also suggest that GimC and TRiC make essential contributions to the compartmentation of protein folding in the eukaryotic cytosol. Kinetic analysis of actin folding and chaperone interactions indicate that GimC acts on or after TRiC in the folding pathway
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A remarkable and detailed examination of the in vivo substrates of GroEL, including the identification by mass spectroscopy of over 50 abundant endogenous substrates. These proteins do not share a common consensus sequence, but instead are significantly enriched for a specific multiple α/β/α domain architecture. Another intriguing finding of this report is the identification of a number of pre-existing proteins that return continually to GroEL throughout the course of their lifetime
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An analysis of yeast mitochondrial Hsp60 and Hsp10 function in protein folding using loss-of-function alleles in each gene. Interestingly, similar, but nonidentical, proteins became aggregated owing to loss of function in either Hsp60 or Hsp10
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