Identification of lysine succinylation as a new post-translational modification

Zhihong Zhang, Minjia Tan, Zhongyu Xie, Lunzhi Dai, Yue Chen, Yingming Zhao

Research output: Contribution to journalArticlepeer-review

387 Scopus citations


Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially identified by mass spectrometry and protein sequence alignment. The identified succinyllysine peptides derived from in vivo proteins were verified by western blot analysis, in vivo labeling with isotopic succinate, MS/MS and HPLC coelution of their synthetic counterparts. We further show that lysine succinylation is evolutionarily conserved and that this PTM responds to different physiological conditions. Our study also implies that succinyl-CoA might be a cofactor for lysine succinylation. Given the apparent high abundance of lysine succinylation and the significant structural changes induced by this PTM, it is expected that lysine succinylation has important cellular functions.

Original languageEnglish (US)
Pages (from-to)58-63
Number of pages6
JournalNature Chemical Biology
Issue number1
StatePublished - Jan 2011
Externally publishedYes

Bibliographical note

Funding Information:
We would like to thank Z. Cheng and Z. Wang for their assistance during the course of this study. This work was supported by US National Institutes of Health grants to Y.Z.

Fingerprint Dive into the research topics of 'Identification of lysine succinylation as a new post-translational modification'. Together they form a unique fingerprint.

Cite this