Department of Biochemistry, College of Medicine, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Epigenetics. 2009 Oct 1;4(7):429-33. doi: 10.4161/epi.4.7.9787. Epub 2009 Oct 10.
Recent studies on the lysine methylation of histones have moved rapidly thanks to the discoveries of a variety of histone lysine methyltransferases. Histone lysine methylation is known to either activate or repress gene expression depending upon the position and status of the methylated lysine residue. Recently, an increasing number of lysine methyltransferases have been identified to modify non-histone proteins. Among those enzymes, the most extensively studied is Set9, a SET domain-containing lysine methyltransferase. Set9 was initially found to target histone H3 lysine 4 for monomethylation and was subsequently shown to target a variety of non-histone proteins, especially transcription-related factors. Functional studies revealed that Set9-mediated methylation of different non-histone proteins leads to distinct biological consequences, most of which point to protein stability. Here we summarize the latest findings on the effects of Set9-mediated lysine methylation on the stability of non-histone proteins.
近年来，由于各种组蛋白赖氨酸甲基转移酶的发现，组蛋白赖氨酸甲基化的研究进展迅速。组蛋白赖氨酸甲基化可根据甲基化赖氨酸残基的位置和状态激活或抑制基因表达。最近，越来越多的赖氨酸甲基转移酶被鉴定为修饰非组蛋白。在这些酶中，研究最广泛的是 Set9，一种含有 SET 结构域的赖氨酸甲基转移酶。最初发现 Set9 靶向组蛋白 H3 赖氨酸 4 进行单甲基化，随后发现它还靶向多种非组蛋白，特别是转录相关因子。功能研究表明，Set9 介导的不同非组蛋白的甲基化导致不同的生物学后果，其中大多数与蛋白质稳定性有关。在这里，我们总结了 Set9 介导的赖氨酸甲基化对非组蛋白稳定性影响的最新发现。
