TY - JOUR
T1 - Lysine succinylation and lysine malonylation in histones
AU - Xie, Zhongyu
AU - Dai, Junbiao
AU - Dai, Lunzhi
AU - Tan, Minjia
AU - Cheng, Zhongyi
AU - Wu, Yeming
AU - Boeke, Jef D.
AU - Zhao, Yingming
PY - 2012/5
Y1 - 2012/5
N2 - 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.
AB - 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.
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U2 - 10.1074/mcp.M111.015875
DO - 10.1074/mcp.M111.015875
M3 - Article
C2 - 22389435
AN - SCOPUS:84861163510
SN - 1535-9476
VL - 11
SP - 100
EP - 107
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
IS - 5
ER -