Lysine Succinylation and Lysine Malonylation in Histones
Lysine Succinylation and Lysine Malonylation in Histones
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DOI：
10.1074/mcp.m111.015875
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发表时间：
2012-05-01
影响因子：
7
通讯作者：
Zhao, Yingming
中科院分区：
文献类型：
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作者：
Xie, Zhongyu;Dai, Junbiao;Zhao, Yingming
组蛋白翻译后修饰（PTM）对基因表达和DNA修复具有重要意义。在这里，我们报告的识别和验证组蛋白中的一种新类型的PTM，赖氨酸琥珀酰化。通过合成肽的MS/MS、HPLC共洗脱和同位素标记来验证鉴定的赖氨酸琥珀酰化组蛋白肽。我们确定了13，7，10和7组蛋白赖氨酸琥珀酰化位点在HeLa，小鼠胚胎成纤维细胞，果蝇S2，和酿酒酵母细胞，分别。我们证明，这种组蛋白PTM是存在于我们检查的所有真核细胞。琥珀酰化位点的突变，然后功能测定表明，组蛋白赖氨酸琥珀酰化可以引起独特的功能后果。我们还确定了一个和两个组蛋白赖氨酸丙二酰化位点在HeLa和S。cerevisiae细胞。因此，我们的研究结果增加了组蛋白PTM的潜在组合多样性，并提出了组蛋白生物学和代谢之间可能的新联系。Molecular & Cellular Proteomics 11：10.1074/mcp. M111.015875，100-107，2012.
Histone protein post-translational modifications (PTMs) are significant for gene expression and DNA repair. Here we report the identification and validation of a new type of PTM in histones, lysine succinylation. The identified lysine succinylated histone peptides were verified by MS/MS of synthetic peptides, HPLC co-elution, and isotopic labeling. We identified 13, 7, 10, and 7 histone lysine succinylation sites in HeLa, mouse embryonic fibroblast, Drosophila S2, and Saccharomyces cerevisiae cells, respectively. We demonstrated that this histone PTM is present in all eukaryotic cells we examined. Mutagenesis of succinylation sites followed by functional assays implied that histone lysine succinylation can cause unique functional consequences. We also identified one and two histone lysine malonylation sites in HeLa and S. cerevisiae cells, respectively. Our results therefore increase potential combinatorial diversity of histone PTMs and suggest possible new connections between histone biology and metabolism. Molecular & Cellular Proteomics 11: 10.1074/mcp.M111.015875, 100-107, 2012.