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J. Biol. Chem., Vol. 282, Issue 45, 33009-33021, November 9, 2007

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Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization^*

From the Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada

PRMT1 is the predominant member of a family of protein arginine methyltransferases (PRMTs) that have been implicated in various cellular processes, including transcription, RNA processing, and signal transduction. It was previously reported that the human PRMT1 pre-mRNA was alternatively spliced to yield three isoforms with distinct N-terminal sequences. Close inspection of the genomic organization in the 5'-end of the PRMT1 gene revealed that it can produce up to seven protein isoforms, all varying in their N-terminal domain. A detailed biochemical characterization of these variants revealed that unique N-terminal sequences can influence catalytic activity as well as substrate specificity. In addition, our results uncovered the presence of a functional nuclear export sequence in PRMT1v2. Finally, we find that the relative balance of PRMT1 isoforms is altered in breast cancer.

Received for publication, May 29, 2007 , and in revised form, August 27, 2007.

^* This work was supported in part by a research grant from The Cancer Research Society Inc. (to J. C.). 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 Figs. 1 and 2.

¹ Supported by a scholarship from Fonds de la Recherche en Santédu Québec.

² Recipient of a Canada Research Chair (Tier 2) in RNA metabolism. To whom correspondence should be addressed: University of Ottawa, Faculty of Medicine, Dept. of Cellular and Molecular Medicine, 451 Smyth Rd., Ottawa, Ontario K1H 8M5, Canada. Tel.: 613-562-5800 (ext. 8660); Fax: 613-562-5636; E-mail: jcote{at}uottawa.ca.

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This article has been cited by other articles:

				J. Sayegh, K. Webb, D. Cheng, M. T. Bedford, and S. G. Clarke Regulation of Protein Arginine Methyltransferase 8 (PRMT8) Activity by Its N-terminal Domain J. Biol. Chem., December 14, 2007; 282(50): 36444 - 36453. [Abstract] [Full Text] [PDF]