Protein lysine methyltransferase G9a acts on non-histone targets
Protein lysine methyltransferase G9a acts on non-histone targets
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DOI：
10.1038/nchembio.88
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发表时间：
2008-06-01
影响因子：
14.8
通讯作者：
Jeltsch, Albert
中科院分区：
文献类型：
--
作者：
Rathert, Philipp;Dhayalan, Arunkumar;Jeltsch, Albert
通过肽阵列的甲基化，我们确定了蛋白质甲基转移酶G9 a的特异性谱。我们发现，它主要识别Arg-Lys序列，其活性受到精氨酸残基甲基化的抑制。使用特异性谱，我们鉴定了G9 a的新的非组蛋白蛋白靶标，包括CDYL 1、WIZ、ACINUS和G9 a（自甲基化），以及来自CSB的肽。我们展示了非组蛋白甲基化的潜在下游信号通路。
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.