Gao Wen-Long, Liu Hong-Lin
College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Yi Chuan. 2007 Dec;29(12):1449-54.
Lysine methylation is an important covalent modification of histone and has fundamental and divers roles in biological processes including regulation of chromatin structure dynamics and gene expression. Recently, a distinct class of histone lysine methyltransferase DOT1 was found to methylate histone H3 lysine79 (H3K79) residue, which is located on the accessible face of the core nucleosome. The DOT1 proteins do not contain a SET domain, a conserved sequence motif found in all previously characterized histone H3 lysine methyltransferases that act on the histone N-termianl tail. The characteristics of DOT1 proteins and H3K79 methylation suggest that they may have important and characteristic functions. Here, we summarize recent advances in specific structure of DOT1 protein, biological functions of DOT1 proteins and H3K79 methylation and trans-histone regulatory1 between histone H2B ubiquitination and H3K79 methylation.
赖氨酸甲基化是组蛋白的一种重要共价修饰，在包括染色质结构动态调控和基因表达在内的生物过程中具有重要且多样的作用。最近，人们发现一类独特的组蛋白赖氨酸甲基转移酶DOT1可使位于核心核小体可及面上的组蛋白H3赖氨酸79（H3K79）残基发生甲基化。DOT1蛋白不含SET结构域，SET结构域是在所有先前已鉴定的作用于组蛋白N末端尾巴的组蛋白H3赖氨酸甲基转移酶中发现的保守序列基序。DOT1蛋白和H3K79甲基化的特征表明它们可能具有重要且独特的功能。在此，我们总结了DOT1蛋白特定结构、DOT1蛋白和H3K79甲基化的生物学功能以及组蛋白H2B泛素化与H3K79甲基化之间的组蛋白间调控的最新进展。
