Strahl B D, Ohba R, Cook R G, Allis C D
Department of Biochemistry, University of Virginia Health Science Center, Charlottesville, VA 22908, USA.
Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14967-72. doi: 10.1073/pnas.96.26.14967.
Studies into posttranslational modifications of histones, notably acetylation, have yielded important insights into the dynamic nature of chromatin structure and its fundamental role in gene expression. The roles of other covalent histone modifications remain poorly understood. To gain further insight into histone methylation, we investigated its occurrence and pattern of site utilization in Tetrahymena, yeast, and human HeLa cells. In Tetrahymena, transcriptionally active macronuclei, but not transcriptionally inert micronuclei, contain a robust histone methyltransferase activity that is highly selective for H3. Microsequence analyses of H3 from Tetrahymena, yeast, and HeLa cells indicate that lysine 4 is a highly conserved site of methylation, which to date, is the major site detected in Tetrahymena and yeast. These data document a nonrandom pattern of H3 methylation that does not overlap with known acetylation sites in this histone. In as much as H3 methylation at lysine 4 appears to be specific to macronuclei in Tetrahymena, we suggest that this modification pattern plays a facilitatory role in the transcription process in a manner that remains to be determined. Consistent with this possibility, H3 methylation in yeast occurs preferentially in a subpopulation of H3 that is preferentially acetylated.
对组蛋白翻译后修饰的研究,尤其是乙酰化修饰,已使人们对染色质结构的动态性质及其在基因表达中的基础作用有了重要认识。而其他共价组蛋白修饰的作用仍知之甚少。为了进一步深入了解组蛋白甲基化,我们研究了其在四膜虫、酵母和人类HeLa细胞中的发生情况及位点利用模式。在四膜虫中,转录活跃的大核而非转录惰性的小核含有一种对H3具有高度选择性的强大组蛋白甲基转移酶活性。对来自四膜虫、酵母和HeLa细胞的H3进行微序列分析表明,赖氨酸4是一个高度保守的甲基化位点,迄今为止,它是在四膜虫和酵母中检测到的主要位点。这些数据证明了H3甲基化的非随机模式,该模式与该组蛋白中已知的乙酰化位点不重叠。鉴于四膜虫中赖氨酸4处的H3甲基化似乎特异于大核,我们认为这种修饰模式以一种有待确定的方式在转录过程中发挥促进作用。与此可能性一致的是,酵母中的H3甲基化优先发生在优先被乙酰化的H3亚群中。