Sharma Rajal, Zhou Ming-Ming
Department of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, 10029.
Protein Sci. 2015 Sep;24(9):1347-59. doi: 10.1002/pro.2711. Epub 2015 Jun 11.
Histones and their modifications play an important role in the regulation of gene transcription. Numerous modifications, such as acetylation, phosphorylation, methylation, ubiquitination, and SUMOylation, have been described. These modifications almost always co-occur and thereby increase the combinatorial complexity of post-translational modification detection. The domains that recognize these histone modifications often occur in tandem in the context of larger proteins and complexes. The presence of multiple modifications can positively or negatively regulate the binding of these tandem domains, influencing downstream cellular function. Alternatively, these tandem domains can have novel functions from their independent parts. Here we summarize structural and functional information known about major tandem domains and their histone binding properties. An understanding of these interactions is key for the development of epigenetic therapy.
组蛋白及其修饰在基因转录调控中发挥着重要作用。已描述了多种修饰,如乙酰化、磷酸化、甲基化、泛素化和小泛素样修饰(SUMOylation)。这些修饰几乎总是同时发生,从而增加了翻译后修饰检测的组合复杂性。识别这些组蛋白修饰的结构域通常在更大的蛋白质和复合物中串联出现。多种修饰的存在可正向或负向调节这些串联结构域的结合,影响下游细胞功能。此外,这些串联结构域可能具有与其独立部分不同的新功能。在此,我们总结了已知的主要串联结构域及其组蛋白结合特性的结构和功能信息。了解这些相互作用是表观遗传治疗发展的关键。