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组蛋白密码是如何起作用的?

How does the histone code work?

作者信息

Cosgrove Michael S, Wolberger Cynthia

机构信息

Department of Biology, Syracuse University, NY 13244, USA.

出版信息

Biochem Cell Biol. 2005 Aug;83(4):468-76. doi: 10.1139/o05-137.

Abstract

Patterns of histone post-translational modifications correlate with distinct chromosomal states that regulate access to DNA, leading to the histone-code hypothesis. However, it is not clear how modification of flexible histone tails leads to changes in nucleosome dynamics and, thus, chromatin structure. The recent discovery that, like the flexible histone tails, the structured globular domain of the nucleosome core particle is also extensively modified adds a new and exciting dimension to the histone-code hypothesis, and calls for the re-examination of current models for the epigenetic regulation of chromatin structure. Here, we review these findings and other recent studies that suggest the structured globular domain of the nucleosome core particle plays a key role regulating chromatin dynamics.

摘要

组蛋白翻译后修饰模式与调节DNA可及性的不同染色体状态相关,从而产生了组蛋白密码假说。然而,尚不清楚柔性组蛋白尾巴的修饰如何导致核小体动力学变化,进而引起染色质结构改变。最近发现,与柔性组蛋白尾巴一样,核小体核心颗粒的结构化球状结构域也被广泛修饰,这为组蛋白密码假说增添了新的、令人兴奋的维度,并要求重新审视当前关于染色质结构表观遗传调控的模型。在这里,我们综述了这些发现以及其他近期研究,这些研究表明核小体核心颗粒的结构化球状结构域在调节染色质动力学中起关键作用。

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