Identification of lysine 37 of histone H2B as a novel site of methylation.
Identification of lysine 37 of histone H2B as a novel site of methylation.
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DOI：
10.1371/journal.pone.0016244
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发表时间：
2011-01-13
期刊：
影响因子：
3.7
通讯作者：
Strahl BD
中科院分区：
文献类型：
--
作者：
Gardner KE;Zhou L;Parra MA;Chen X;Strahl BD
最近的技术进步使得基于质谱的高度复杂的组蛋白密码研究成为可能，该研究预测组蛋白翻译后修饰（PTM）的组合会导致由识别这些标记的效应蛋白介导的确定的生物学结果。尽管在组蛋白 PTM 的鉴定和表征方面已经取得了重大进展，但要充分了解组蛋白代码的复杂性，需要完全理解所有可能对其有贡献的修饰。在这里，我们使用自上而下的质谱方法来识别全长组蛋白的 PTM，结果发现组蛋白 H2B 的赖氨酸 37 在芽殖酵母酿酒酵母中被二甲基化。通过生成修饰特异性抗体和在假定的甲基化位点存在突变的酵母菌株，我们提供了该标记在体内存在的证据。重要的是，我们证明这种赖氨酸残基在进化过程中高度保守，并提供了这种甲基化事件也发生在高等真核生物中的证据。通过确定组蛋白甲基化的新位点，这项研究增强了我们对有助于染色质功能的复杂组蛋白修饰的整体理解。
Recent technological advancements have allowed for highly-sophisticated mass spectrometry-based studies of the histone code, which predicts that combinations of post-translational modifications (PTMs) on histone proteins result in defined biological outcomes mediated by effector proteins that recognize such marks. While significant progress has been made in the identification and characterization of histone PTMs, a full appreciation of the complexity of the histone code will require a complete understanding of all the modifications that putatively contribute to it. Here, using the top-down mass spectrometry approach for identifying PTMs on full-length histones, we report that lysine 37 of histone H2B is dimethylated in the budding yeast Saccharomyces cerevisiae. By generating a modification-specific antibody and yeast strains that harbor mutations in the putative site of methylation, we provide evidence that this mark exist in vivo. Importantly, we show that this lysine residue is highly conserved through evolution, and provide evidence that this methylation event also occurs in higher eukaryotes. By identifying a novel site of histone methylation, this study adds to our overall understanding of the complex number of histone modifications that contribute to chromatin function.
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