PRMT9 is a Type II methyltransferase that methylates the splicing factor SAP145

Yanzhong Yang (), Andrea Hadjikyriacou, Zheng Xia, Sitaram Gayatri, Daehoon Kim, Cecilia Zurita-Lopez, Ryan Kelly, Ailan Guo, Wei Li, Steven G. Clarke and Mark T. Bedford ()
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Yanzhong Yang: The University of Texas MD Anderson Cancer Center
Andrea Hadjikyriacou: Molecular Biology Institute, University of California Los Angeles
Zheng Xia: Baylor College of Medicine
Sitaram Gayatri: The University of Texas MD Anderson Cancer Center
Daehoon Kim: The University of Texas MD Anderson Cancer Center
Cecilia Zurita-Lopez: Molecular Biology Institute, University of California Los Angeles
Ryan Kelly: Molecular Biology Institute, University of California Los Angeles
Ailan Guo: Cell Signaling Technology Inc.
Wei Li: Baylor College of Medicine
Steven G. Clarke: Molecular Biology Institute, University of California Los Angeles
Mark T. Bedford: The University of Texas MD Anderson Cancer Center

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The human genome encodes a family of nine protein arginine methyltransferases (PRMT1–9), whose members can catalyse three distinct types of methylation on arginine residues. Here we identify two spliceosome-associated proteins—SAP145 and SAP49—as PRMT9-binding partners, linking PRMT9 to U2 snRNP maturation. We show that SAP145 is methylated by PRMT9 at arginine 508, which takes the form of monomethylated arginine (MMA) and symmetrically dimethylated arginine (SDMA). PRMT9 thus joins PRMT5 as the only mammalian enzymes capable of depositing the SDMA mark. Methylation of SAP145 on Arg 508 generates a binding site for the Tudor domain of the Survival of Motor Neuron (SMN) protein, and RNA-seq analysis reveals gross splicing changes when PRMT9 levels are attenuated. These results identify PRMT9 as a nonhistone methyltransferase that primes the U2 snRNP for interaction with SMN.

Date: 2015
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DOI: 10.1038/ncomms7428

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