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

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

Research output: Contribution to journalArticle

68 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1032-1034
Number of pages3
JournalScience
Volume308
Issue number5724
DOIs
StatePublished - May 13 2005

    Fingerprint

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. https://doi.org/10.1126/science.1109247