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  • Title: Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.
    Author: Hundley HA, Walter W, Bairstow S, Craig EA.
    Journal: Science; 2005 May 13; 308(5724):1032-4. PubMed ID: 15802566.
    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.
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