Role of histone acetylation in the assembly and modulation of chromatin structures.
Role of histone acetylation in the assembly and modulation of chromatin structures.
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DOI：
10.3727/000000001783992687
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
A. Annunziato;Hansen Jc
中科院分区：
文献类型：
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作者：
A. Annunziato;Hansen Jc
核心组蛋白 N 末端“尾”结构域的乙酰化现在被认为是调节染色质功能状态的高度保守机制。以下文章探讨了乙酰化在两个极其重要的细胞过程中的可能作用：复制偶联核小体组装和染色质高级结构中的可逆转变。在描述了新合成的组蛋白的乙酰化以及可能涉及的乙酰转移酶之后，概述了组蛋白八聚体组装。然后描述了我们目前对体内染色质组装因素的理解。详细介绍了组蛋白尾部及其乙酰化在核小体组装中的功能的遗传和生化研究，然后分析了组蛋白脱乙酰化在新复制的染色质成熟中的重要性。在最后一节中，讨论了组蛋白尾部结构域在染色质高级结构中的参与，以及组蛋白乙酰化在染色质折叠中的作用。结论性意见中提出了对未来研究的建议。
The acetylation of the core histone N-terminal "tail" domains is now recognized as a highly conserved mechanism for regulating chromatin functional states. The following article examines possible roles of acetylation in two critically important cellular processes: replication-coupled nucleosome assembly, and reversible transitions in chromatin higher order structure. After a description of the acetylation of newly synthesized histones, and of the likely acetyltransferases involved, an overview of histone octamer assembly is presented. Our current understanding of the factors thought to assemble chromatin in vivo is then described. Genetic and biochemical investigations of the function the histone tails, and their acetylation, in nucleosome assembly are detailed, followed by an analysis of the importance of histone deacetylation in the maturation of newly replicated chromatin. In the final section the involvement of the histone tail domains in chromatin higher order structures is addressed, along with the role of histone acetylation in chromatin folding. Suggestions for future research are offered in the concluding remarks.