Biochemical analysis of the catalytic activity of protein arginine methyltransferase 1 (PRMT1)

• Main Authors: Yu-Ling Lu, 呂玉琳
• Other Authors: Wey-Jing Lin
• Format: Others
• Language: zh-TW
• Published: 2002
• Online Access: http://ndltd.ncl.edu.tw/handle/85887402131896497397

碩士 === 國立陽明大學 === 生物藥學研究所 === 90 === Protein arginine methyltransferase 1 (PRMT1) is a type I protein arginine methyltransferase, which can catalyze the formation of asymmetric ω-NG,N’G-dimethylarginine residues by transferring methyl groups from S-adenosyl-L-methionine to guanidine groups of arginine residues in a variety of eukaryotic proteins. To study the catalytic properties of PRMT1, we have successfully purified recombinant GST-PRMT1 and showed that GST-PRMT1 was enzymatically active using Trx-hnRNP A2 as a substrate. The kinetic properties of GST-PRMT1 with either Trx-hnRNP A2 or a peptide substrate containing RGG motif have been examined. Divalent cations showed differential effects on methylation of Trx-hnRNP A2 and the peptide substrate by GST-PRMT1. These suggested a potential regulation of PRMT1 activity through metal ions in cells.