Protein lysine methyltransferase G9a acts on non-histone targets

被引：275

作者：

Rathert, Philipp ^{[1
]}

Dhayalan, Arunkumar ^{[1
]}

Murakami, Marie ^{[2
,3
]}

Zhang, Xing ^{[4
]}

Tamas, Raluca ^{[1
,5
]}

Jurkowska, Renata ^{[1
]}

Komatsu, Yasuhiko ^{[6
]}

Shinkai, Yoichi ^{[2
,3
]}

Cheng, Xiaodong ^{[4
]}

Jeltsch, Albert ^{[1
]}

机构：

[1] Jacobs Univ Bremen, Sch Sci & Engn, Biochem Lab, D-28759 Bremen, Germany

[2] Kyoto Univ, Res Ctr Infect Dis, Inst Virus Res, Sakyo Ku, Kyoto 6068507, Japan

[3] Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068507, Japan

[4] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

[5] Jacobs Univ Bremen, Sch Sci & Engn, Biochem & Cell Biol Program, D-28759 Bremen, Germany

[6] Adv Life Sci Inst Inc, R&D Div, Wako, Saitama 3510112, Japan

来源：

NATURE CHEMICAL BIOLOGY | 2008年 / 4卷 / 06期

关键词：

D O I：

10.1038/nchembio.88

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

By methylation of peptide arrays, we determined the specificity profile of the protein methyltransferase G9a. We show that it mostly recognizes an Arg-Lys sequence and that its activity is inhibited by methylation of the arginine residue. Using the specificity profile, we identified new non-histone protein targets of G9a, including CDYL1, WIZ, ACINUS and G9a (automethylation), as well as peptides derived from CSB. We demonstrate potential downstream signaling pathways for methylation of non-histone proteins.

引用

页码：344 / 346

页数：3

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