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J. Biol. Chem., Vol. 280, Issue 38, 32890-32896, September 23, 2005

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PRMT8, a New Membrane-bound Tissue-specific Member of the Protein Arginine Methyltransferase Family^*

Jaeho Lee1, Joyce Sayegh1, Jeremy Daniel, Steven Clarke, Supported by Grant GM26020 from the National Institutes of Health2, and Mark T. Bedford, Supported by NIEHS National Institutes of Health Grant ES077843

From the Science Park-Research Division, The University of Texas M. D. Anderson Cancer Center, Smithville, Texas 78957 and The Molecular Biology Institute and Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095-1569

Protein arginine methylation is a common post-translational modification that has been implicated in signal transduction, RNA processing, transcriptional regulation, and DNA repair. A search of the human genome for additional members of the protein arginine N-methyltransferase (PRMT) family of enzymes has identified a gene on chromosome 12 that we have termed PRMT8. This novel enzyme is most closely related to PRMT1, although it has a distinctive N-terminal region. The unique N-terminal end harbors a myristoylation motif, and we have shown here that PRMT8 is indeed modified by the attachment of a myristate to the glycine residue after the initiator methionine. The myristoylation of PRMT8 results in its association with the plasma membrane. The second singular property of PRMT8 is its tissue-specific expression pattern; it is largely expressed in the brain. A glutathione S-transferase fusion protein of PRMT8 has type I PRMT activity, catalyzing the formation of -N^G-monomethylated and asymmetrically -N^G,N^G-dimethylated arginine residues on a recombinant glycine- and arginine-rich substrate. PRMT8 is thus an active arginine methyltransferase that is membrane-associated and tissue-specific, two firsts for this family of enzymes.

Received for publication, June 27, 2005 , and in revised form, July 26, 2005.

^* This work was supported in part by Grant G-1495 (to M. T. B.) from the Welch Foundation. 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 These authors contributed equally to this work.

² To whom correspondence may be addressed. Tel.: 310-825-8754; E-mail: clarke{at}mbi.ucla.edu. ³ To whom correspondence may be addressed. Tel.: 512-237-9539; E-mail: mtbedford{at}mdanderson.org.

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