SGD Paper 
Hundley HA, et al. (2005) Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 308(5724):1032-4
Abstract: The existence of specialized molecular chaperones that interact directly with ribosomes is well-established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J-protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multi-purpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multi-functional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.
| Status: Published | Type: Journal Article | PubMed ID: 15802566 |
Topics addressed in this paper
Number of different genes curated to this paper: 2
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