作者: Zhongyu Xie , Junbiao Dai , Lunzhi Dai , Minjia Tan , Zhongyi Cheng
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摘要: Histone protein post-translational modifications (PTMs) are significant for gene expression and DNA repair. Here we report the identification validation of a new type PTM in histones, lysine succinylation. The identified succinylated histone peptides were verified by MS/MS synthetic peptides, HPLC co-elution, isotopic labeling. We 13, 7, 10, 7 succinylation sites HeLa, mouse embryonic fibroblast, Drosophila S2, Saccharomyces cerevisiae cells, respectively. demonstrated that this is present all eukaryotic cells examined. Mutagenesis followed functional assays implied can cause unique consequences. also one two malonylation HeLa S. Our results therefore increase potential combinatorial diversity PTMs suggest possible connections between biology metabolism.