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论文题目: Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro
英文论文题目: Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro
第一作者: Li, HT; Gong, T; Zhou, Z; Liu, YT; Cao, XW; He, YN; Chen, CD; Zhou, JQ
英文第一作者: Li, HT; Gong, T; Zhou, Z; Liu, YT; Cao, XW; He, YN; Chen, CD; Zhou, JQ
联系作者: Chen, CD (reprint author), Univ Chinese Acad Sci, Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol,Shanghai Inst Biol Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.
英文联系作者: Chen, CD (reprint author), Univ Chinese Acad Sci, Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol,Shanghai Inst Biol Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.
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发表年度: 2015
卷: 467
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页码: 507-515
摘要: Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs' substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1's activity. Interestingly, the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules. Our results suggest an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates.
英文摘要: Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs' substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1's activity. Interestingly, the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules. Our results suggest an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates.
刊物名称: BIOCHEMICAL JOURNAL
英文刊物名称: BIOCHEMICAL JOURNAL
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学科: Biochemistry & Molecular Biology
英文学科: Biochemistry & Molecular Biology
影响因子: 4.396
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论文类别: Article
英文论文类别: Article
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