Journal
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE
Volume 22, Issue 3, Pages 309-315Publisher
SPANDIDOS PUBL LTD
DOI: 10.3892/ijmm_00000024
Keywords
EWS; arginine-glycine-glycine repeats; protein arginine methyltransferase 8; protein arginine methylation; asymmetric dimethylarginine
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Funding
- 21st Century COE Program
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- University of Tsukuba Special Research Program
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EWS, a pro-oncoprotein which is encoded by the Ewing sarcoma (EWS) gene, contains arginine-glycine-glycine repeats (RGG box) in its COOH-terminus. We previously found that the RGG box of EWS is a target for dimethylation catalyzed by protein arginine methyltransferases (PRMTs). Although it has been observed that arginine residues in EWS are dimethylated in vivo, the endogenous enzyme(s) responsible for this reaction have not been identified to date. In the present study, we determined that EWS was physically associated wish PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thinlayer chromatography. These results suggested that EWS is a substrate for PRMT8, as efficient as for PRMT1.
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