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A more recent version of this article appeared on January 1, 2003
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Submitted on August 12, 2002
Revised on September 12, 2002
Accepted on September 20, 2002
1 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, Medicine, Microbiology and Immunology, McGill University, Montréal, Québec, H3T 1E2
2 M.D. Anderson Cancer Center, Department of Carcinogenesis, University of Texas, Smithville, Texas 78957
* Corresponding author. E-mail address: stephane.richard{at}mcgill.ca.
RNA binding proteins often contain multiple arginine glycine repeats, a sequence that is frequently methylated by protein arginine methyltransferases. The role of this post-translational modification in the life cycle of RNA binding proteins is not well understood. Here we report that Sam68, a heteronuclear ribonucleoprotein (hnRNP) K homology (KH) domain containing RNA binding protein, associates with and is methylated in vivo by the protein arginine N-methyltransferase 1. Sam68 contains asymmetrical dimethylarginines near its proline motif P3 as assessed by using a novel asymmetrical dimethylarginine-specific antibody and mass spectrometry. Deletion of the methylation sites and the use of methylase inhibitors resulted in Sam68 accumulation in the cytoplasmic. Sam68 was also detected in the cytoplasm of PRMT1-deficient embryonic stem cells. Although the cellular function of Sam68 is unknown, it has been shown to export unspliced HIV RNAs. Cells treated with methylase inhibitors prevented the ability of Sam68 to export unspliced HIV RNAs. Other KH domain RNA binding proteins including SLM-1, SLM-2, QKI-5, GRP33 and hnRNP K were also methylated in vivo. These findings demonstrate that RNA binding proteins are in vivo substrates for PRMT1 and their methylation is essential for their proper localization and function.
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