Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
Molecules. 2018 Oct 12;23(10):2614. doi: 10.3390/molecules23102614.
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.
真核生物基因组以染色质的形式包装到细胞核中，染色质是基因组 DNA 和组蛋白的复合物。染色质结构的调节对所有依赖于 DNA 的过程都至关重要，涉及到组蛋白蛋白的广泛翻译后修饰。这些修饰可以通过称为组蛋白读取域的组蛋白结合亚域“读出”。已经鉴定出大量的读取域，并发现它们选择性地识别一系列组蛋白翻译后修饰，以便在其底物处靶向、保留或调节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读取域被鉴定为还具有核酸结合活性。在这篇综述中，我们总结了目前已知结合核酸的组蛋白读取域，重点介绍了结合的分子机制以及 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关联和调节中的功能意义。我们提出，核酸结合与组蛋白结合一样具有功能重要性，并且很大一部分尚未经过测试的读取域将具有核酸结合能力。
