Wozniak Glenn G, Strahl Brian D
Curriculum in Genetics and Molecular Biology, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Curriculum in Genetics and Molecular Biology, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA; Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Biochim Biophys Acta. 2014 Dec;1839(12):1353-61. doi: 10.1016/j.bbagrm.2014.03.002. Epub 2014 Mar 12.
Histones and their posttranslational modifications (PTMs) play an important role in regulating DNA-templated processes. While some PTMs directly modulate chromatin architecture via charge effects, others rely on the action of reader or effector proteins that can recognize and bind the modification to fulfill distinct cellular outcomes. One PTM that has been well studied with regard to reader proteins is histone lysine methylation - a PTM linked to many DNA-templated processes including transcription, DNA replication and DNA repair. In this review, we summarize the current understanding of how histone lysine methylation is read during the process of active transcription. We also describe how the interpretation of lysine methylation fits into a larger, more complex 'code' of histone PTMs to modulate chromatin structure and function. These insights take into account emerging concepts in the field in an effort to help facilitate future studies.
组蛋白及其翻译后修饰（PTMs）在调控DNA模板化过程中发挥着重要作用。虽然一些PTMs通过电荷效应直接调节染色质结构，但其他PTMs则依赖于读取蛋白或效应蛋白的作用，这些蛋白能够识别并结合修饰以实现不同的细胞结果。在读取蛋白方面得到充分研究的一种PTM是组蛋白赖氨酸甲基化——一种与包括转录、DNA复制和DNA修复在内的许多DNA模板化过程相关的PTM。在本综述中，我们总结了目前对活性转录过程中组蛋白赖氨酸甲基化如何被读取的理解。我们还描述了赖氨酸甲基化的解读如何融入更大、更复杂的组蛋白PTM“密码”中，以调节染色质结构和功能。这些见解考虑了该领域的新兴概念，以期有助于促进未来的研究。
