Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.
Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.
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DOI：
10.1016/j.jbc.2021.100939
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发表时间：
2021-08
期刊：
影响因子：
--
通讯作者：
Wilkins MR
中科院分区：
文献类型：
--
作者：
Separovich RJ;Wilkins MR
组蛋白赖氨酸甲基化是调节真核转录的关键表观遗传修饰。在这里，我们全面回顾了芽殖酵母和模型真核生物酿酒酵母中组蛋白甲基化网络的功能和调控。首先，我们概述了酵母组蛋白上发现的赖氨酸甲基化位点（H3K4me1/2/3、H3K36me1/2/3、H3K79me1/2/3 和 H4K5/8/12me1），并讨论了它们的生物学和细胞作用。接下来，我们详细介绍了一组减少但进化上保守的甲基转移酶（Set1p、Set2p、Dot1p 和 Set5p）和去甲基酶（Jhd1p、Jhd2p、Rph1p 和 Gis1p），这些酶已知可控制芽殖酵母细胞中的组蛋白赖氨酸甲基化。具体来说，我们说明了甲基化酶的结构域，并强调了它们各自的功能和分子相互作用所需的结构特征。最后，我们讨论了酵母组蛋白甲基化酶翻译后修饰的普遍性，以及磷酸化、乙酰化和泛素化如何成为酶功能的关键调节因子。我们注意到，鉴于所有甲基化位点和同源酶都是已知的，酶上的大多数磷酸位点都是已知的，并且由于酵母中蛋白激酶的数量不多，激酶与磷酸位点的映射是容易处理的，因此将组蛋白甲基化网络完全连接到细胞的信号系统是可能的。展望未来，我们预计修饰组蛋白甲基化机制的丰富多样的翻译后修饰将解释围绕这个复杂的表观遗传网络的功能和动力学的许多未解决的问题。
Histone lysine methylation is a key epigenetic modification that regulates eukaryotic transcription. Here, we comprehensively review the function and regulation of the histone methylation network in the budding yeast and model eukaryote, Saccharomyces cerevisiae. First, we outline the lysine methylation sites that are found on histone proteins in yeast (H3K4me1/2/3, H3K36me1/2/3, H3K79me1/2/3, and H4K5/8/12me1) and discuss their biological and cellular roles. Next, we detail the reduced but evolutionarily conserved suite of methyltransferase (Set1p, Set2p, Dot1p, and Set5p) and demethylase (Jhd1p, Jhd2p, Rph1p, and Gis1p) enzymes that are known to control histone lysine methylation in budding yeast cells. Specifically, we illustrate the domain architecture of the methylation enzymes and highlight the structural features that are required for their respective functions and molecular interactions. Finally, we discuss the prevalence of post-translational modifications on yeast histone methylation enzymes and how phosphorylation, acetylation, and ubiquitination in particular are emerging as key regulators of enzyme function. We note that it will be possible to completely connect the histone methylation network to the cell’s signaling system, given that all methylation sites and cognate enzymes are known, most phosphosites on the enzymes are known, and the mapping of kinases to phosphosites is tractable owing to the modest set of protein kinases in yeast. Moving forward, we expect that the rich variety of post-translational modifications that decorates the histone methylation machinery will explain many of the unresolved questions surrounding the function and dynamics of this intricate epigenetic network.
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影响因子：
3.8
作者：
Bostelman, Lindsey J.;Keller, Andrew M.;Thompson, Jeffrey S.
通讯作者：
Thompson, Jeffrey S.
影响因子：
16
作者：
Altaf, Mohammed;Utley, Rhea T.;Cote, Jacques
通讯作者：
Cote, Jacques
DOI：
10.1073/pnas.51.5.786
发表时间：
1964-01-01
影响因子：
11.1
作者：
ALLFREY, VG;FAULKNER, R;MIRSKY, AE
通讯作者：
MIRSKY, AE
影响因子：
2.7
作者：
Hérissant L;Moehle EA;Bertaccini D;Van Dorsselaer A;Schaeffer-Reiss C;Guthrie C;Dargemont C
通讯作者：
Dargemont C
影响因子：
16.6
作者：
Bae, Hyun Jin;Dubarry, Marion;Buratowski, Stephen
通讯作者：
Buratowski, Stephen