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Protein arginine methyltransferase 1 methylates SF2/ASF at arginine
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Abstract:
Objective:To investigate the arginine (Arg) sites in splicing factor 2/alternative splicing factor (SF2/ASF) methylated by protein arginine methyltransferase 1 (PRMT1). Methods: Wildtype and Arg93, Arg97, Arg109 mutant SF2/ASF plasmids were constructed, and GSTPRMT1, GSTSF2/ASF and arginine mutant GSTSF2/ASF fusion proteins were induced and purified. Methylation activity of PRMT1 on wildtype or mutant SF2/ASF protein and methylated sites of SF2/ASF were examined by methylation assay. The effect of SF2/ASF methylation on its subcellular localization was analyzed by immunofluorescence assay.Results: PRMT1 induced methylation of SF2/ASF at arginine, and PRMT1 did not methylate SF2/ASF when SF2/ASF was mutant at Arg93, Arg97 or Arg109, with Arg97 mutation showing the most profound inhibitory effect. Methylation of SF2/ASF did not affect its subcellular localization.Conclusion: SF2/ASF is a newly identified substrate of PRMT1; Arg93, Arg97 and Arg 109 are the three methylation sites in SF2/ASF, and Arg97 is the main methylation site. Methylation of SF2/ASF does not affect its subcellular localization.
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Project Supported:
Supported by the Modern Medical Technology Major Project of National 863 Program（No.2006AA02A405）; the Modern Medical Technology Key Project of National 863 Program (No. 2006AA02Z4Z2)
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