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Originally published in Science Express on 31 March 2005
Science 13 May 2005:
Vol. 308. no. 5724, pp. 1032 - 1034
DOI: 10.1126/science.1109247
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Reports

Human Mpp11 J Protein: Ribosome-Tethered Molecular Chaperones Are Ubiquitous

Heather A. Hundley,1,2* William Walter,1 Shawn Bairstow,2 Elizabeth A. Craig1{dagger}

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.

1 Department of Biochemistry, 433 Babcock Drive, University of Wisconsin–Madison, Madison, WI 53706, USA.
2 Graduate Program in Biomolecular Chemistry, University of Wisconsin–Madison, Madison, WI 53706, USA.

Published online 31 March 2005

Include this information when citing this paper.

* Present address: Department of Biochemistry and Howard Hughes Medical Institute, University of Utah, Salt Lake City, UT 84132, USA.

{dagger} To whom correspondence should be addressed. E-mail: ecraig{at}wisc.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)