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蛋白质赖氨酸甲基转移酶G9a作用于非组蛋白靶点。

Protein lysine methyltransferase G9a acts on non-histone targets.

作者信息

Rathert Philipp, Dhayalan Arunkumar, Murakami Marie, Zhang Xing, Tamas Raluca, Jurkowska Renata, Komatsu Yasuhiko, Shinkai Yoichi, Cheng Xiaodong, Jeltsch Albert

机构信息

Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.

出版信息

Nat Chem Biol. 2008 Jun;4(6):344-6. doi: 10.1038/nchembio.88. Epub 2008 Apr 27.

Abstract

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.

摘要

通过对肽阵列进行甲基化,我们确定了蛋白质甲基转移酶G9a的特异性谱。我们发现它主要识别精氨酸-赖氨酸序列,并且其活性会受到精氨酸残基甲基化的抑制。利用该特异性谱,我们鉴定出了G9a的新的非组蛋白蛋白质靶点,包括CDYL1、WIZ、ACINUS和G9a(自身甲基化),以及源自CSB的肽段。我们证明了非组蛋白蛋白质甲基化的潜在下游信号通路。

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