Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli.

ABSTRACT: Lysine succinylation is a newly identified protein post-translational modification pathway present in both prokaryotic and eukaryotic cells. However, succinylation substrates and regulatory enzyme(s) remain largely unknown, hindering the biological study of this modification. Here we report the identification of 2,580 bacterial lysine succinylation sites in 670 proteins and 2,803 lysine acetylation (Kac) sites in 782 proteins, representing the first lysine succinylation dataset and the largest Kac dataset in wild-type E. coli. We quantified dynamic changes of the lysine succinylation and Kac substrates in response to high glucose. Our data showed that high-glucose conditions led to more lysine-succinylated proteins and enhanced the abundance of succinyllysine peptides more significantly th

SUBMITTER: Colak G 

PROVIDER: S-EPMC3861704 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature