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J. Biol. Chem., Vol. 281, Issue 52, 40096-40106, December 29, 2006

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RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes^*

Kimio J. Tanaka, Kenji Ogawa, Masatoshi Takagi, Naoko Imamoto, Ken Matsumoto¹, and Masafumi Tsujimoto

From the Laboratory of Cellular Biochemistry and Laboratory of Cellular Dynamics, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

mRNAs in eukaryotic cells are presumed to always associate with a set of proteins to form mRNPs. In Xenopus oocytes, a large pool of maternal mRNAs is masked from the translational apparatus as storage mRNPs. Here we identified Xenopus RAP55 (xRAP55) as a component of RNPs that associate with FRGY2, the principal component of maternal mRNPs. RAP55 is a member of the Scd6 or Lsm14 family. RAP55 localized to cytoplasmic foci in Xenopus oocytes and the processing bodies (P-bodies) in cultured human cells: in the latter cells, RAP55 is an essential constituent of the P-bodies. We isolated xRAP55-containing complexes from Xenopus oocytes and identified xRAP55-associated proteins, including a DEAD-box protein, Xp54, and a protein arginine methyltransferase, PRMT1. Recombinant xRAP55 repressed translation, together with Xp54, in an in vitro translation system. In addition, xRAP55 repressed translation in oocytes when tethered with a reporter mRNA. Domain analyses revealed that the N-terminal region of RAP55, including the Lsm domain, is important for the localization to P-bodies and translational repression. Taken together, our results suggest that xRAP55 is involved in translational repression of mRNA as a component of storage mRNPs.

Received for publication, September 25, 2006 , and in revised form, October 26, 2006.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB257699 [GenBank] .

^* This work was supported in part by a grant-in-aid from the Ministry of Education, Culture, Sports, Science, and Technology, Japan, and by a grant for Bioarchitect Research Program from RIKEN. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental text, references, and Figs. S1-S4.

¹ To whom correspondence should be addressed. Tel.: 81-48-467-9764; Fax: 81-48-462-4670; E-mail: matsumok{at}riken.jp.

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