Abstract
Background: Newly discovered protein arginine methyltransferase 9 (PRMT9) modulates alternative splicing by methylation of SF3B2. Results: Biochemical probes of PRMT9 and its substrate protein revealed domains and residues required for methylation. Conclusion: PRMT9 is unique among PRMTs in its narrow range of methyl-accepting substrates. Significance: Understanding PRMT9 catalysis will help elucidate how it may control the activity of SF3B2 and other potential endogenous substrates.
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CITATION STYLE
Hadjikyriacou, A., Yang, Y., Espejo, A., Bedford, M. T., & Clarke, S. G. (2015). Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2. Journal of Biological Chemistry, 290(27), 16723–16743. https://doi.org/10.1074/jbc.M115.659433
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