Lysine succinylation and lysine malonylation in histones

Zhongyu Xie, Junbiao Dai, Lunzhi Dai, Minjia Tan, Zhongyi Cheng, Yeming Wu, Jef D. Boeke, Yingming Zhao

    Research output: Contribution to journalArticle

    Abstract

    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.

    Original languageEnglish (US)
    Pages (from-to)100-107
    Number of pages8
    JournalMolecular and Cellular Proteomics
    Volume11
    Issue number5
    DOIs
    StatePublished - May 2012

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Biochemistry
    • Molecular Biology

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  • Cite this

    Xie, Z., Dai, J., Dai, L., Tan, M., Cheng, Z., Wu, Y., Boeke, J. D., & Zhao, Y. (2012). Lysine succinylation and lysine malonylation in histones. Molecular and Cellular Proteomics, 11(5), 100-107. https://doi.org/10.1074/mcp.M111.015875