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

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  • Yanzhong Yang

    (The University of Texas MD Anderson Cancer Center
    Beckman Research Institute, City of Hope 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)

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.

Suggested Citation

  • Yanzhong Yang & Andrea Hadjikyriacou & Zheng Xia & Sitaram Gayatri & Daehoon Kim & Cecilia Zurita-Lopez & Ryan Kelly & Ailan Guo & Wei Li & Steven G. Clarke & Mark T. Bedford, 2015. "PRMT9 is a Type II methyltransferase that methylates the splicing factor SAP145," Nature Communications, Nature, vol. 6(1), pages 1-12, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7428
    DOI: 10.1038/ncomms7428
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    Cited by:

    1. Xuemei Bai & Chao Sui & Feng Liu & Tian Chen & Lei Zhang & Yi Zheng & Bingyu Liu & Chengjiang Gao, 2022. "The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Lei Shen & Xiaokuang Ma & Yuanyuan Wang & Zhihao Wang & Yi Zhang & Hoang Quoc Hai Pham & Xiaoqun Tao & Yuehua Cui & Jing Wei & Dimitri Lin & Tharindumala Abeywanada & Swanand Hardikar & Levon Halabeli, 2024. "Loss-of-function mutation in PRMT9 causes abnormal synapse development by dysregulation of RNA alternative splicing," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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