Binary switches and modification cassettes in histone biology and beyond
Binary switches and modification cassettes in histone biology and beyond
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DOI：
10.1038/nature02017
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发表时间：
2003-10-02
期刊：
影响因子：
64.8
通讯作者：
Allis, CD
中科院分区：
文献类型：
--
作者：
Fischle, W;Wang, YM;Allis, CD
大量的组蛋白翻译后修饰已被描述，其他修饰位点仍在被发现。虽然现在已经建立了某些组蛋白修饰与不同生物现象之间的许多直接和间接联系，但缺乏理解这些共价修饰的极端密度和多样性的概念。在这里，我们正式引入了本地化的“二进制开关”和“修饰盒”作为组蛋白生物学中的新概念，阐明了可能控制不同修饰模式的生物学读出的机制。具体来说，我们的假设为稳定组蛋白修饰的动态读出提供了缺失的模型，并为文献中嵌入的几个长期存在的问题提供了解释。我们的想法可能也适用于非组蛋白，并开放直接的实验检验。
An immense number of post-translational modifications on histone proteins have been described and additional sites of modification are still being uncovered. Whereas many direct and indirect connections between certain histone modifications and distinct biological phenomena have now been established, concepts for comprehending the extreme density and variety of these covalent modifications are lacking. Here, we formally introduce localized 'binary switches' and 'modification cassettes' as new concepts in histone biology, elucidating mechanisms that might govern the biological readout of distinct modification patterns. Specifically, our hypotheses provide missing models for the dynamic readout of stable histone modifications and offer explanations for several long-standing questions embedded in the literature. Our ideas might also apply to non-histone proteins and are open to direct experimental examination.