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J. Biol. Chem., Vol. 280, Issue 31, 28476-28483, August 5, 2005

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Tudor Domains Bind Symmetrical Dimethylated Arginines^*

Jocelyn Côté and Stéphane Richard, Investigator of the CIHR

From the Terry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital and Departments of Oncology and Medicine, McGill University, Montréal, Québec H3T 1E2, Canada

The Tudor domain is an 60-amino acid structure motif in search of a function. Herein we show that the Tudor domains of the spinal muscular atrophy gene product SMN, the splicing factor 30 kDa (SPF30), and the Tudor domain-containing 3 (TDRD3) proteins interacted with arginine-glycine-rich motifs in a methylarginine-dependent manner. The Tudor domains also associated with methylarginine-containing cellular proteins, providing evidence that methylated arginines represent physiological ligands for this protein module. In addition, we report that spliceosomal small nuclear ribonucleoprotein particles core Sm proteins accumulated in the cytoplasm when arginine methylation was inhibited with adenosine dialdehyde or in the presence of an excessive amount of unmethylated arginine-glycine-rich peptides. These data provide in vivo evidence in support of a role for arginine methylation in the proper assembly and localization of spliceosomal Sm proteins.

Received for publication, December 20, 2004 , and in revised form, May 31, 2005.

^* This work was supported by Grant MOP-67070 from the Canadian Institutes of Health Research (CIHR) (to S. R.) and a research grant from the Families of Spinal Muscular Atrophy (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.

New Investigator of the CIHR. Present address: Dept. of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada.

To whom correspondence should be addressed: Lady Davis Inst., 3755 Côte-Ste-Catherine Rd., Montréal, Québec, Canada H3T 1E2. Tel.: 514-340-8260; Fax: 514-340-8295; E-mail: stephane.richard{at}mcgill.ca.

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