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 multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.||PubMed ID: 15802566|
Topics addressed in this paper
Number of different genes curated to this paper: 2
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