Rona Germana B, Eleutherio Elis C A, Pinheiro Anderson S
Department of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, 21941-909, Brazil.
Biophys Rev. 2016 Mar;8(1):63-74. doi: 10.1007/s12551-015-0190-6. Epub 2016 Jan 14.
Chromatin plays an important role in gene transcription control, cell cycle progression, recombination, DNA replication and repair. The fundamental unit of chromatin, the nucleosome, is formed by a DNA duplex wrapped around an octamer of histones. Histones are susceptible to various post-translational modifications, covalent alterations that change the chromatin status. Lysine methylation is one of the major post-translational modifications involved in the regulation of chromatin function. The PWWP domain is a member of the Royal superfamily that functions as a chromatin methylation reader by recognizing both DNA and histone methylated lysines. The PWWP domain three-dimensional structure is based on an N-terminal hydrophobic β-barrel responsible for histone methyl-lysine binding, and a C-terminal α-helical domain. In this review, we set out to discuss the most recent literature on PWWP domains, focusing on their structural features and the mechanisms by which they specifically recognize DNA and histone methylated lysines at the level of the nucleosome.
染色质在基因转录调控、细胞周期进程、重组、DNA复制和修复中发挥着重要作用。染色质的基本单位核小体由缠绕在组蛋白八聚体周围的DNA双链形成。组蛋白易受各种翻译后修饰的影响，这些共价改变会改变染色质状态。赖氨酸甲基化是参与染色质功能调控的主要翻译后修饰之一。PWWP结构域是皇家超家族的成员之一，通过识别DNA和组蛋白甲基化赖氨酸发挥染色质甲基化阅读器的作用。PWWP结构域的三维结构基于负责结合组蛋白甲基赖氨酸的N端疏水β桶和C端α螺旋结构域。在本综述中，我们着手讨论关于PWWP结构域的最新文献，重点关注其结构特征以及它们在核小体水平特异性识别DNA和组蛋白甲基化赖氨酸的机制。
