Not all Is SET for Methylation: Evolution of Eukaryotic Protein Methyltransferases
Not all Is SET for Methylation: Evolution of Eukaryotic Protein Methyltransferases
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并非一切都适合甲基化：真核蛋白质甲基转移酶的进化
DOI：
10.1007/978-1-0716-2481-4_1
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发表时间：
2022
影响因子：
--
通讯作者：
Freitag M
中科院分区：
文献类型：
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作者：
Erlendson AA;Freitag M
对构成核小体的典型组蛋白（H2A、H2B、H3和H4）的动态翻译后修饰控制与DNA的酶促交易的所有方面。在过去的20年里，组蛋白甲基化已经被大量研究，在过去的十年里，我们对特定组蛋白精氨酸和赖氨酸残基上的单个甲基化事件的控制和功能的机械理解已经得到了很大的改善，这是由优秀的新工具和方法驱动的。在这里，我们将总结什么是已知的分布和一些功能的蛋白质甲基转移酶从所有主要的真核超组。主要结论是，蛋白质，特别是组蛋白，甲基化是一个古老的过程。许多分类群在所有的超群已经失去了一些亚家族的蛋白质精氨酸甲基转移酶（PRMT）和深入研究的SET结构域赖氨酸甲基转移酶（KMT）。随着时间的推移，出现了新的亚家族，特别是SET结构域蛋白。我们使用H3K27和H3K36甲基化之间的相互作用作为组成“组蛋白密码”的组蛋白修饰的复杂电路的一个例子，我们讨论了一个最近的例子（草履虫Ezl1），为如何现存的酶，可能类似于更古老的SET域KMT能够修改两个赖氨酸残基，在植物，真菌和动物中具有不同的功能。SET结构域的复杂性KMT功能在植物和动物谱系中得到了充分研究，不仅由基因复制，但也收购了新的DNA和组蛋白结合域在某些亚科。
Dynamic posttranslational modifications to canonical histones that constitute the nucleosome (H2A, H2B, H3, and H4) control all aspects of enzymatic transactions with DNA. Histone methylation has been studied heavily for the past 20 years, and our mechanistic understanding of the control and function of individual methylation events on specific histone arginine and lysine residues has been greatly improved over the past decade, driven by excellent new tools and methods. Here, we will summarize what is known about the distribution and some of the functions of protein methyltransferases from all major eukaryotic supergroups. The main conclusion is that protein, and specifically histone, methylation is an ancient process. Many taxa in all supergroups have lost some subfamilies of both protein arginine methyltransferases (PRMT) and the heavily studied SET domain lysine methyltransferases (KMT). Over time, novel subfamilies, especially of SET domain proteins, arose. We use the interactions between H3K27 and H3K36 methylation as one example for the complex circuitry of histone modifications that make up the “histone code,” and we discuss one recent example (ParameciumEzl1) for how extant enzymes that may resemble more ancient SET domain KMTs are able to modify two lysine residues that have divergent functions in plants, fungi, and animals. Complexity of SET domain KMT function in the well-studied plant and animal lineages arose not only by gene duplication but also acquisition of novel DNA- and histone-binding domains in certain subfamilies.