Symmetrical modification within a nucleosome is not required globally for histone lysine methylation
Symmetrical modification within a nucleosome is not required globally for histone lysine methylation
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DOI：
10.1038/embor.2011.6
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发表时间：
2011-03-01
期刊：
影响因子：
7.7
通讯作者：
Zhu, Bing
中科院分区：
文献类型：
--
作者：
Chen, Xiuzhen;Xiong, Jun;Zhu, Bing
每个核小体中存在两个核心组蛋白的拷贝;然而，不知道核小体中的两个组蛋白是否需要在相同的赖氨酸残基处对称甲基化。我们报告说，对于大多数赖氨酸甲基化状态，野生型组蛋白配对突变，unmethylatable组蛋白在单核体具有可比的甲基化水平散装组蛋白。我们的研究结果表明，对称的组蛋白甲基化是不需要在全球范围内。然而，野生型H4组蛋白与不可甲基化的H4 K20 R组蛋白配对显示H4 K20 me 2和H4 K20 me 3水平降低，表明这些修饰的一些部分可能对称存在，并且介导这些修饰的酶可能在一定程度上有利于具有预甲基化H4 K20的核小体底物。
Two copies of each core histone exist in every nucleosome; however, it is not known whether both histones within a nucleosome are required to be symmetrically methylated at the same lysine residues. We report that for most lysine methylation states, wild-type histones paired with mutant, unmethylatable histones in mononucleosomes have comparable methylation levels to bulk histones. Our results indicate that symmetrical histone methylation is not required on a global scale. However, wild-type H4 histones paired with unmethylatable H4K20R histones showed reduced levels of H4K20me2 and H4K20me3, suggesting that some fractions of these modifications might exist symmetrically, and enzymes mediating these modifications might, to some extent, favour nucleosome substrates with premethylated H4K20.