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Published Online March 31, 2005
Science DOI: 10.1126/science.1109247

Reports

Submitted on December 29, 2004
Accepted on February 23, 2005

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

Heather A. Hundley 1, William Walter 2, Shawn Bairstow 3, Elizabeth A. Craig 2*

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

* To whom correspondence should be addressed.
Elizabeth A. Craig , E-mail: ecraig{at}wisc.edu

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 multi-purpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multi-functional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.


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