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

J. Biol. Chem., Vol. 282, Issue 23, 16917-16923, June 8, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/23/16917    most recent M609778200v1 Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Swiercz, R. Articles by Bedford, M. T. Search for Related Content PubMed PubMed Citation Articles by Swiercz, R. Articles by Bedford, M. T. Social Bookmarking                      What's this?

Ribosomal Protein rpS2 Is Hypomethylated in PRMT3-deficient Mice^*

From the University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, Smithville, Texas 78957

PRMT3 is a type I arginine methyltransferase that resides in the cytoplasm. A large proportion of this cystosolic PRMT3 is found associated with ribosomes. It is tethered to the ribosomes through its interaction with rpS2, which is also its substrate. Here we show that mouse embryos with a targeted disruption of PRMT3 are small in size but survive after birth and attain a normal size in adulthood, thus displaying Minute-like characteristics. The ribosome protein rpS2 is hypomethylated in the absence of PRMT3, demonstrating that it is a bona fide, in vivo PRMT3 substrate that cannot be modified by other PRMTs. Finally, the levels 40 S, 60 S, and 80 S monosomes and polyribosomes are unaffected by the loss of PRMT3, but there are additional as yet unidentified proteins that co-fractionate with ribosomes that are also dedicated PRMT3 substrates.

Received for publication, October 17, 2006 , and in revised form, April 16, 2007.

^* 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.

¹ Supported by the Welch Foundation Grant G-1495. To whom correspondence should be addressed. Tel.: 512-237-9539; 512-237-2475; E-mail: mtbedford{at}mdanderson.org.

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

This article has been cited by other articles:

				I. Goulet, S. Boisvenue, S. Mokas, R. Mazroui, and J. Cote TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules Hum. Mol. Genet., October 1, 2008; 17(19): 3055 - 3074. [Abstract] [Full Text] [PDF]

				A. Perreault, C. Bellemer, and F. Bachand Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2 Nucleic Acids Res., September 27, 2008; (2008) gkn625v1. [Abstract] [Full Text] [PDF]

				K. Fronz, S. Otto, K. Kolbel, U. Kuhn, H. Friedrich, A. Schierhorn, A. G. Beck-Sickinger, A. Ostareck-Lederer, and E. Wahle Promiscuous Modification of the Nuclear Poly(A)-binding Protein by Multiple Protein-arginine Methyltransferases Does Not Affect the Aggregation Behavior J. Biol. Chem., July 18, 2008; 283(29): 20408 - 20420. [Abstract] [Full Text] [PDF]

				M. T. Bedford Arginine methylation at a glance J. Cell Sci., December 15, 2007; 120(24): 4243 - 4246. [Full Text] [PDF]