组蛋白八聚体
组蛋白密码
核小体
生物
组蛋白
组蛋白H2A
组蛋白甲基化
组蛋白H1
组蛋白甲基转移酶
染色质
组蛋白H4
遗传学
细胞生物学
计算生物学
DNA
基因
DNA甲基化
基因表达
标识
DOI:10.1016/0955-0674(91)90070-f
摘要
The past year has seen major advances in our understanding of histone and nucleosome structure and function. Direct DNA mapping and thermodynamic experiments have finally provided conclusive evidence that the histones impose an altered helical pitch on the DNA as it is wrapped on the surface of the core histone octamer. Further, it is now clear that lysine acetylation in the amino-terminal domains of histones H3 and H4 can alter the topology of the DNA in chromatin and probably influence its higher-order folding. Genetic experiments reported in the past year have provided a wealth of new information on histone structure and function, including the identification of the peptide domain of histone H4 that is necessary for permanent gene repression, the confirmation that nucleosome structure is critical for centromere function, and evidence that histone acetylation plays a significant role in chromosome dynamics.
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