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J. Biol. Chem., Vol. 278, Issue 49, 49119-49128, December 5, 2003

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Cpc2/RACK1 Is a Ribosome-associated Protein That Promotes Efficient Translation in Schizosaccharomyces pombe^*

Boris Shor, Jimmy Calaycay¶, Julie Rushbrook¶, and Maureen McLeod||

From the Morse Institute for Molecular Genetics, Department of Microbiology and Immunology, the ^¶Department of Biochemistry, and the Program in Molecular and Cellular Biology, State University of New York Downstate Medical Center, Brooklyn, New York 11203-2098

Cpc2/RACK1 is a highly conserved WD domain protein found in all eucaryotes. Cpc2/RACK1 functions on mammalian signal transduction pathways most notably as an adaptor protein for the II protein kinase C isozyme. In single cell eucaryotes, Cpc2/RACK1 regulates growth, differentiation, and entry into G₀ stationary phase. The exact biochemical function of Cpc2/RACK1 is unknown. Here, we provide evidence that Cpc2 is associated with the ribosome. Using immunoaffinity purification, we isolated ribosomal proteins in association with Cpc2/RACK1. Polysome and ribosomal subunit analysis using velocity gradient centrifugation of cell lysates demonstrated that Cpc2 co-sediments with the 40 S ribosomal subunit and with polysomes. Conditions known to disrupt ribosome structure alter sedimentation of the ribosome and of Cpc2/RACK1 coordinately. Loss of cpc2 does not dramatically alter the rate of cellular protein synthesis but causes a decrease in the steady state level of numerous proteins, some of which regulate methionine metabolism. Whereas real time PCR analysis demonstrated that transcriptional mechanisms are responsible for down-regulation of some of these proteins, one protein, ribosomal protein L25, is probably regulated at the level of translation.

Received for publication, April 15, 2003 , and in revised form, September 11, 2003.

^* This work was supported by the State University of New York, American Heart Association Grant 9850102T, and National Institutes of Health Grant 5RO1GM56875. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Johnson and Johnson Pharmaceutical Research and Development, 1000 Route 202, Raritan, NJ 08869.

^|| To whom correspondence should be addressed. Tel.: 718-270-3321; Fax: 718-270-2656; E-mail: mmcleod{at}netmail.hscbklyn.edu.

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