Peters Antoine H F M, Schübeler Dirk
Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH 4058 Basel, Switzerland.
Curr Opin Cell Biol. 2005 Apr;17(2):230-8. doi: 10.1016/j.ceb.2005.02.006.
Nucleosomal histones can be methylated in vivo at multiple residues and defined methylation patterns are related to distinct functional readouts of chromosomal DNA. Histone methylation has emerged as an important post-translational modification involved in transcriptional regulation and genome integrity. Recent progress in determining the cis and trans determinants of this process revealed multiple roles for histone methylation in epigenetic memory of active and silent states. The analysis of imprinted, X-linked and heterochromatic sequences disclosed mechanistic similarities for heritable transcriptional repression, pointing to a common mode of action. Moreover, the view of histone methylation as a stable modification has recently been challenged by studies revealing a number of pathways that are capable of removing histone methylation. Thus, in addition to having great in vivo complexity, this modification appears more dynamic then was previously thought.
核小体组蛋白在体内多个残基处可发生甲基化,特定的甲基化模式与染色体DNA的不同功能解读相关。组蛋白甲基化已成为一种重要的翻译后修饰,参与转录调控和基因组完整性。在确定该过程的顺式和反式决定因素方面的最新进展揭示了组蛋白甲基化在活跃和沉默状态的表观遗传记忆中的多种作用。对印记、X连锁和异染色质序列的分析揭示了可遗传转录抑制的机制相似性,指向一种共同的作用模式。此外,最近的研究对组蛋白甲基化作为一种稳定修饰的观点提出了挑战,这些研究揭示了许多能够去除组蛋白甲基化的途径。因此,除了在体内具有极大的复杂性外,这种修饰似乎比以前认为的更具动态性。