Fingerman Ian M, Du Hai-Ning, Briggs Scott D
Epigenetics. 2008 Sep;3(5):237-42. doi: 10.4161/epi.3.5.6869. Epub 2008 Sep 26.
Covalent post-translational modifications of histones have been demonstrated to participate in a wide array of cellular processes, including regulation of gene transcription, gene repression, DNA double strand break repair and mitosis. Regulation of how these covalent modifications, and the implications of this regulation, are currently of great interest. It has been long known that the addition and/or removal of these chromatin modifications are catalyzed by various classes of chromatin modifying enzymes, such as histone acetyltransferases/deacetylases and histone methyltransferases/demethylases. More recently, it has been demonstrated that the addition or removal of these modifications can be dependant upon other existing modifications, both in cis, from within the same histone, or in trans, contributed from another histone. The first trans-histone regulatory event was observed in , and influenced histone lysine methylation. This review will give insight into and summarize newly identified trans-histone pathways as a regulatory mechanism for histone lysine methylation.
组蛋白的共价翻译后修饰已被证明参与了广泛的细胞过程，包括基因转录调控、基因抑制、DNA双链断裂修复和有丝分裂。目前，这些共价修饰的调控方式及其意义备受关注。长期以来，人们已知这些染色质修饰的添加和/或去除是由各类染色质修饰酶催化的，如组蛋白乙酰转移酶/去乙酰化酶和组蛋白甲基转移酶/去甲基化酶。最近，已证明这些修饰的添加或去除可能取决于其他现有的修饰，这些修饰既可以是同一组蛋白内的顺式作用，也可以是另一组蛋白贡献的反式作用。首次观察到的反式组蛋白调控事件发生在[具体时间未给出]，并影响了组蛋白赖氨酸甲基化。本综述将深入探讨并总结新发现的反式组蛋白途径，作为组蛋白赖氨酸甲基化的一种调控机制。
