articleMolecular & Cellular ProteomicsMar 5, 2012HYBRID OA

Lysine Succinylation and Lysine Malonylation in Histones

University of Chicago · Johns Hopkins University · +3 more institutions

PubMed
Indexed incrossrefdoajpubmed

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…

No related works found for this paper.