Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains.

Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains.
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阅读不仅仅是组蛋白:读取器结构域之间核酸结合的流行率。

DOI:
10.3390/molecules23102614
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发表时间:
2018-10-12
期刊:
Molecules (Basel, Switzerland)
影响因子:
--
通讯作者:
Musselman CA
Musselman CA
中科院分区:
其他
文献类型:
--
作者:
Weaver TM;Morrison EA;Musselman CA

文献摘要

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真核基因组以染色质(基因组DNA和组蛋白的复合物)的形式包装到细胞核中。染色质结构调节对于所有DNA模板化过程是至关重要的,并且涉及组蛋白的广泛翻译后修饰。这些修饰可以被称为组蛋白阅读器结构域的组蛋白结合亚结构域“读出”。已经鉴定了大量的阅读器结构域,并发现其选择性地识别组蛋白翻译后修饰的阵列,以便靶向、保留或调节其底物处的染色质修饰和重塑复合物。有趣的是,越来越多的这些组蛋白阅读器结构域被鉴定为也具有核酸结合活性。在这篇综述中,我们提出了一个总结的组蛋白阅读器域目前已知的结合核酸,重点是结合的分子机制和DNA和组蛋白识别之间的相互作用。此外,我们强调了核酸结合在染色质结合和调节中的功能意义。我们认为核酸结合在功能上与组蛋白结合一样重要,并且大部分尚未测试的阅读器结构域将具有核酸结合能力。
The eukaryotic genome is packaged into the cell nucleus in the form of chromatin, a complex of genomic DNA and histone proteins. Chromatin structure regulation is critical for all DNA templated processes and involves, among many things, extensive post-translational modification of the histone proteins. These modifications can be “read out” by histone binding subdomains known as histone reader domains. A large number of reader domains have been identified and found to selectively recognize an array of histone post-translational modifications in order to target, retain, or regulate chromatin-modifying and remodeling complexes at their substrates. Interestingly, an increasing number of these histone reader domains are being identified as also harboring nucleic acid binding activity. In this review, we present a summary of the histone reader domains currently known to bind nucleic acids, with a focus on the molecular mechanisms of binding and the interplay between DNA and histone recognition. Additionally, we highlight the functional implications of nucleic acid binding in chromatin association and regulation. We propose that nucleic acid binding is as functionally important as histone binding, and that a significant portion of the as yet untested reader domains will emerge to have nucleic acid binding capabilities.