HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

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

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/52/40096    most recent M609059200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tanaka, K. J. Articles by Tsujimoto, M. Search for Related Content PubMed PubMed Citation Articles by Tanaka, K. J. Articles by Tsujimoto, M. Social Bookmarking                      What's this?

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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Minshall, M. Kress, D. Weil, and N. Standart Role of p54 RNA Helicase Activity and Its C-terminal Domain in Translational Repression, P-body Localization and Assembly Mol. Biol. Cell, May 1, 2009; 20(9): 2464 - 2472. [Abstract] [Full Text] [PDF]

				F. Tritschler, A. Eulalio, S. Helms, S. Schmidt, M. Coles, O. Weichenrieder, E. Izaurralde, and V. Truffault Similar Modes of Interaction Enable Trailer Hitch and EDC3 To Associate with DCP1 and Me31B in Distinct Protein Complexes Mol. Cell. Biol., November 1, 2008; 28(21): 6695 - 6708. [Abstract] [Full Text] [PDF]

				H. Kawahara, T. Imai, H. Imataka, M. Tsujimoto, K. Matsumoto, and H. Okano Neural RNA-binding protein Musashi1 inhibits translation initiation by competing with eIF4G for PABP J. Cell Biol., October 17, 2008; 181(4): 639 - 653. [Abstract] [Full Text] [PDF]

				S. L. Noble, B. L. Allen, L. K. Goh, K. Nordick, and T. C. Evans Maternal mRNAs are regulated by diverse P body-related mRNP granules during early Caenorhabditis elegans development J. Cell Biol., August 11, 2008; 182(3): 559 - 572. [Abstract] [Full Text] [PDF]

				P. R. Boag, A. Atalay, S. Robida, V. Reinke, and T. K. Blackwell Protection of specific maternal messenger RNAs by the P body protein CGH-1 (Dhh1/RCK) during Caenorhabditis elegans oogenesis J. Cell Biol., August 11, 2008; 182(3): 543 - 557. [Abstract] [Full Text] [PDF]

				N. Minshall, M. H. Reiter, D. Weil, and N. Standart CPEB Interacts with an Ovary-specific eIF4E and 4E-T in Early Xenopus Oocytes J. Biol. Chem., December 28, 2007; 282(52): 37389 - 37401. [Abstract] [Full Text] [PDF]

				Z. R. Belak and N. Ovsenek Assembly of the Yin Yang 1 Transcription Factor into Messenger Ribonucleoprotein Particles Requires Direct RNA Binding Activity J. Biol. Chem., December 28, 2007; 282(52): 37913 - 37920. [Abstract] [Full Text] [PDF]

				F. Tritschler, A. Eulalio, V. Truffault, M. D. Hartmann, S. Helms, S. Schmidt, M. Coles, E. Izaurralde, and O. Weichenrieder A Divergent Sm Fold in EDC3 Proteins Mediates DCP1 Binding and P-Body Targeting Mol. Cell. Biol., December 15, 2007; 27(24): 8600 - 8611. [Abstract] [Full Text] [PDF]

				A. Eulalio, I. Behm-Ansmant, D. Schweizer, and E. Izaurralde P-Body Formation Is a Consequence, Not the Cause, of RNA-Mediated Gene Silencing Mol. Cell. Biol., June 1, 2007; 27(11): 3970 - 3981. [Abstract] [Full Text] [PDF]

				A. Jakymiw, K. M. Pauley, S. Li, K. Ikeda, S. Lian, T. Eystathioy, M. Satoh, M. J. Fritzler, and E. K. L. Chan The role of GW/P-bodies in RNA processing and silencing J. Cell Sci., April 15, 2007; 120(8): 1317 - 1323. [Abstract] [Full Text] [PDF]