Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".

Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".
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DOI:
10.1002/cbic.201000474
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发表时间:
2011-01-24
期刊:
影响因子:
3.2
通讯作者:
Denu, John M.
Denu, John M.
中科院分区:
生物学3区
文献类型:
--
作者:
Oliver, Samuel S.;Denu, John M.

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组蛋白将DNA组织成动态的染色质结构,并调节转录、修复和复制等过程。染色质功能和结构的控制部分是通过组蛋白的可逆翻译后修饰(PTM)来实现的。组蛋白H3的最大N末端区域含有高密度的可修饰残基。在这篇综述中,我们重点讨论了H3N-末端的组蛋白修饰状态与识别这些状态的结合模块之间的动态相互作用。具体来说,我们将讨论辅助修饰对H3K4unmod/ME3结合模块的影响(特别是H3R2甲基化、H3T3磷酸化和H3T6磷酸化)。新出现的证据表明,组蛋白PTM的行为不太像一种严格的‘代码’,而更像一种‘语言’,这更好地说明了上下文的重要性。以雄激素受体介导的基因激活为例,我们提出了一个模型,说明H3N末端PTM的结合性质和识别这些表观遗传修饰的复合体如何控制基因表达。
Histone proteins organize DNA into dynamic chromatin structures and regulate processes such as transcription, repair and replication. Control of chromatin function and structure is mediated in part by reversible posttranslational modifications (PTMs) on histones. The most N-terminal region of histone H3 contains a high density of modifiable residues. In this review, we focus on the dynamic interplay between histone modification states on the H3 N-terminus and the binding modules that recognize these states. Specifically, we will discuss the effect of auxiliary modifications to H3K4unmod/me3 binding modules (specifically H3R2 methylation, H3T3 phosphorylation and H3T6 phosphorylation). Emerging evidence suggests that histone PTMs behave less like a strict ‘code’, but rather like a ‘language’, which better illustrates the importance of context. Using androgen receptor-mediated gene activation as an example, we propose a model for how the combinatorial nature of PTMs on the H3 N-terminus and the complexes that recognize these epigenetic modifications control gene expression.
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