Human Mpp11 J protein: Ribosome-tethered molecular chaperons are ubiquitous

Heather A. Hundley, William Walter, Shawn Bairstow, Elizabeth A. Craig

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68 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1032-1034
Number of pages3
Issue number5724
StatePublished - May 13 2005


ASJC Scopus subject areas

  • General

Cite this

Hundley, H. A., Walter, W., Bairstow, S., & Craig, E. A. (2005). Human Mpp11 J protein: Ribosome-tethered molecular chaperons are ubiquitous. Science, 308(5724), 1032-1034.