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首页> 外文期刊>Molecular & cellular proteomics: MCP >Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry.
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Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry.

机译：使用串联质谱图映射组蛋白变体MacroH2A1的翻译后修饰。

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摘要

Post-translational histone modifications modulate chromatin-templated processes and therefore affect cellular proliferation, growth, and development. Although post-translational modifications on the core histones have been under intense investigation for several years, the modifications on variant histones are poorly understood. We used tandem mass spectrometry to identify covalent modifications on a histone H2A variant, macroH2A1.2. MacroH2A1.2 can be monoubiquitinated; however, the site of monoubiquitination has not been documented. In this study we used green fluorescent protein-tagged macroH2A1.2 to determine that Lys(115) is a site of ubiquitination. In addition, we found that this variant H2A is methylated on the epsilon amino group of lysine residues Lys(17), Lys(122), and Lys(238) and phosphorylated on Thr(128). Three of these modifications were also found to be present in the endogenous protein by mass spectrometric analysis. These results provide the first direct evidence that multiple post-translational modifications are imposed on macroH2A1.2, suggesting that, like canonical H2A, this variant H2A is subject to regulation by combinatorial use of covalent modifications.
机译：翻译后的组蛋白修饰调节染色质模板化的过程，因此影响细胞的增殖，生长和发育。尽管已经对核心组蛋白的翻译后修饰进行了深入研究数年，但对变异组蛋白的修饰却知之甚少。我们使用串联质谱法来鉴定组蛋白H2A变体macroH2A1.2的共价修饰。 MacroH2A1.2可以单泛素化;但是，单泛素化的位置尚未记录。在这项研究中，我们使用绿色荧光蛋白标记的macroH2A1.2来确定Lys（115）是泛素化的位点。另外，我们发现该变体H2A在赖氨酸残基Lys（17），Lys（122）和Lys（238）的ε氨基上甲基化并且在Thr（128）上磷酸化。通过质谱分析还发现这些修饰中的三个存在于内源蛋白质中。这些结果提供了第一个直接证据，证明对macroH2A1.2进行了多个翻译后修饰，这表明，与规范H2A一样，该变体H2A受到组合使用共价修饰的调节。

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