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Dynamics of histone acetylation in vivo. A function for acetylation turnover?

机译:体内组蛋白乙酰化的动力学。乙酰化转换功能?

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Histone acetylation, discovered more than 40 years ago, is a reversible modification of lysines within the amino-terminal domain of core histones. Amino-terminal histone domains contribute to the compaction of genes into repressed chromatin fibers. It is thought that their acetylation causes localized relaxation of chromatin as a necessary but not sufficient condition for processes that repackage DNA such as transcription, replication, repair, recombination, and sperm formation. While increased histone acetylation enhances gene transcription and loss of acetylation represses and silences genes, the function of the rapid continuous or repetitive acetylation and deacetylation reactions with half-lives of just a few minutes remains unknown. Thirty years of in vivo measurements of acetylation turnover and rates of change in histone modification levels have been reviewed to identify common chromatin characteristics measured by distinct protocols. It has now become possible to look across a wider spectrum of organisms than ever before and identify common features. The rapid turnover rates in transcriptionally active and competent chromatin are one such feature. While ubiquitously observed, we still do not know whether turnover itself is linked to chromatin transcription beyond its contribution to rapid changes towards hyper- or hypoacetylation of nucleosomes. However, recent experiments suggest that turnover may be linked directly to steps in gene transcription, interacting with nucleosome remodeling complexes.
机译:40多年前发现的组蛋白乙酰化是核心组蛋白氨基末端域内赖氨酸的可逆修饰。氨基末端的组蛋白结构域有助于将基因压缩成抑制的染色质纤维。认为它们的乙酰化会导致染色质的局部松弛,这是重新包装DNA的过程(例如转录,复制,修复,重组和精子形成)的必要条件,但不是充分条件。虽然增加的组蛋白乙酰化作用增强了基因转录,乙酰化作用的丧失抑制并沉默了基因,但快速持续或重复的乙酰化作用和脱乙酰化反应的作用(半衰期只有几分钟)仍然未知。回顾了三十年来的体内乙酰化转化率和组蛋白修饰水平变化率的体内测量,以鉴定通过不同方案测量的常见染色质特征。现在,有可能比以往任何时候都可以查看更广泛的生物体并识别共同特征。转录活性和感受态染色质的快速周转率就是这样的特征之一。尽管无处不在,但我们仍不知道营业额本身是否与染色质转录有关,而不仅仅是染色质转录对核小体过度乙酰化或低乙酰化的快速变化的贡献。然而,最近的实验表明,营业额可能直接与基因转录步骤相关,并与核小体重构复合物相互作用。

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