Chemical synthesis of the ubiquitinated form of histone H3 and its effect on DNA methyltransferase 1
Chemical synthesis of the ubiquitinated form of histone H3 and its effect on DNA methyltransferase 1
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DOI：
10.1002/psc.3200
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发表时间：
2019-09
影响因子：
2.1
通讯作者：
T. Kawakami;Yuichi Mishima;Masaya Takazawa;H. Hojo;I. Suetake
中科院分区：
文献类型：
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作者：
T. Kawakami;Yuichi Mishima;Masaya Takazawa;H. Hojo;I. Suetake
构成核小体核心的组蛋白的翻译后修饰在基因调控中起着重要作用。泛素化就是这样一种修饰。我们先前报道了具有异肽模拟结构的泛素化组蛋白H3的合成。在这份报告中，我们描述了制备的泛素化组蛋白H3肽与天然的异肽结构，这表明略弱的影响，DNA甲基转移酶1的酶活性比以前的泛素化H3肽类似物。这些发现表明，天然结构对于确定功能机制是重要的，尽管泛素化H3肽类似物可以模拟原始泛素化H3的作用。我们还报道了泛素化的全长组蛋白H3的成功制备。
Posttranslational modifications of histone proteins, which form nucleosome cores, play an important role in gene regulation. Ubiquitination is one such modification. We previously reported on the synthesis of ubiquitinated histone H3 with an isopeptide mimetic structure. In this report, we describe the preparation of ubiquitinated histone H3 peptides with a native isopeptide structure, which showed a slightly weaker effect on the enzymatic activity of DNA methyltransferase 1 than the previous ubiquitinated H3 peptide analogs. These findings show that a native structure is important for determining the mechanism of the function, although ubiquitinated H3 peptide analogs can mimic the role of the original ubiquitinated H3. We also report on the successful preparation of the ubiquitinated full length histone H3.