Newcastle Cancer Centre at the Northern Institute for Cancer Research; Newcastle University, Newcastle upon Tyne, England.
Epigenetics. 2013 May;8(5):457-63. doi: 10.4161/epi.24451. Epub 2013 Apr 27.
Lysine methylation of histones and non-histone proteins has emerged in recent years as a posttranslational modification with wide-ranging cellular implications beyond epigenetic regulation. The molecular interactions between lysine methyltransferases and their substrates appear to be regulated by posttranslational modifications surrounding the lysine methyl acceptor. Two very interesting examples of this cross-talk between methyl-lysine sites are found in the SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain-containing lysine methyltransferases SET7 and SETDB1, whereby the histone H3 trimethylated on lysine 4 (H3K4 (me3) ) modification prevents methylation by SETDB1 on H3 lysine 9 (H3K9) and the histone H3 trimethylated on lysine 9 (H3K9 (me3) ) modification prevents methylation by SET7 on H3K4. A similar cross-talk between posttranslational modifications regulates the functions of non-histone proteins such as the tumor suppressor p53 and the DNA methyltransferase DNMT1. Herein, in cis effects of acetylation, phosphorylation, as well as arginine and lysine methylation on lysine methylation events will be discussed.
近年来，组蛋白和非组蛋白赖氨酸甲基化作为一种翻译后修饰，其在表观遗传调控之外的广泛细胞意义已逐渐显现。赖氨酸甲基转移酶与其底物之间的分子相互作用似乎受到赖氨酸甲基受体周围的翻译后修饰的调节。这种赖氨酸甲基化位点之间的交叉对话在 SET（Su(var)3-9、Enhancer-of-zeste、Trithorax）结构域包含的赖氨酸甲基转移酶 SET7 和 SETDB1 中找到了两个非常有趣的例子，其中组蛋白 H3 赖氨酸 4 上的三甲基化（H3K4（me3））修饰阻止了 SETDB1 对 H3 赖氨酸 9（H3K9）的甲基化，而组蛋白 H3 赖氨酸 9 上的三甲基化（H3K9（me3））修饰阻止了 SET7 对 H3K4 的甲基化。类似的翻译后修饰之间的交叉对话调节了非组蛋白的功能，如肿瘤抑制因子 p53 和 DNA 甲基转移酶 DNMT1。在此，将讨论乙酰化、磷酸化以及精氨酸和赖氨酸甲基化对赖氨酸甲基化事件的顺式效应。
