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首页> 外文期刊>Angewandte Chemie >Interaction of Propionylated and Butyrylated Histone H3 Lysine Marks with Brd4 Bromodomains
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Interaction of Propionylated and Butyrylated Histone H3 Lysine Marks with Brd4 Bromodomains

机译:丙酰化和丁酰化的组蛋白H3赖氨酸标记与Brd4溴结构域的相互作用

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摘要

The regulation of eukaryotic gene expression is determined by modifications in the chromatin structure. The highly variable pattern of modifications in the histone chains is described as the histone code. Two sets of histone proteins H2A, H2B, H3, and H4 form the octameric core of each nucleosome. Two turns of genomic DNA are wound around this octameric core to form the packaging of chromatin structures. Histone proteins are subject to a wide array of posttranslational modifications, including methylation, citrul-lination, acetylation, phosphorylation, ubiquitination, and sumoylation. These histone marks determine the state of chromatin dynamics and remodeling; the study of their specific imprint, which outlasts even cell division, is known as epigenetics.
机译:真核基因表达的调节取决于染色质结构的修饰。组蛋白链中高度可变的修饰模式称为组蛋白代码。两组组蛋白H2A,H2B,H3和H4形成每个核小体的八聚体核心。将两圈基因组DNA缠绕在该八聚体核心周围,以形成染色质结构的包装。组蛋白的翻译后修饰范围很广,包括甲基化,瓜氨酸化,乙酰化,磷酸化,泛素化和磺酰化。这些组蛋白标记决定了染色质动力学和重塑的状态。对它们的特定印记的研究甚至可以持续进行细胞分裂,这种研究被称为表观遗传学。

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