组蛋白H4赖氨酸91乙酰化——一种与染色质组装相关的核心结构域修饰。
Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.
作者信息
Ye Jianxin, Ai Xi, Eugeni Ericka E, Zhang Liwen, Carpenter Laura Rocco, Jelinek Mary A, Freitas Michael A, Parthun Mark R
机构信息
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
出版信息
Mol Cell. 2005 Apr 1;18(1):123-30. doi: 10.1016/j.molcel.2005.02.031.
The acetylation of the NH2-terminal tail of histone H4 by type B histone acetyltransferases (HATs) is involved in the process of chromatin assembly. Histone H4 associated with a nuclear type B HAT complex contains modifications in its globular core domain as well. In particular, acetylation was found at lysine 91. A mutation that alters this residue, which lies in the interface between histone H3/H4 tetramers and H2A/H2B dimers, confers phenotypes consistent with defects in chromatin assembly such as sensitivity to DNA damaging agents and derepression and alteration of silent chromatin structure. In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structure. These results indicate an important role for histone modifications outside the NH2-tail domains in the processes of chromatin assembly, DNA repair, and transcriptional silencing.
B型组蛋白乙酰转移酶（HATs）对组蛋白H4氨基末端尾巴的乙酰化作用参与了染色质组装过程。与核B型HAT复合物相关的组蛋白H4在其球状核心结构域也存在修饰。特别是在赖氨酸91处发现了乙酰化。改变位于组蛋白H3/H4四聚体与H2A/H2B二聚体界面处这一残基的突变，会导致与染色质组装缺陷一致的表型，如对DNA损伤剂敏感、沉默染色质结构的去抑制和改变。此外，这种突变会使组蛋白八聚体不稳定，导致染色质结构缺陷。这些结果表明，在染色质组装、DNA修复和转录沉默过程中，氨基末端尾巴结构域之外的组蛋白修饰具有重要作用。
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