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Title 

The acetylproteome of Gram-positive model bacterium Bacillus subtilis

Authors 

Doo-Il KimB J YuJung-Ae KimY J LeeSoo Keun ChoiSunghyun KangJae Gu Pan

Publisher 

Wiley-Blackwell

Issue Date 

2013

Citation 

Proteomics, vol. 13, no. 10, pp. 1726-1736

Keywords 

AcetylationBacillus subtilisBacteriaEnzymesPTM

Abstract 

Nε-lysine acetylation, a reversible and highly regulated PTM, has been shown to occur in the model Gram-negative bacteria Escherichia coli and Salmonella enterica. Here, we extend this acetylproteome analysis to Bacillus subtilis, a model Gram-positive bacterium. Through anti-acetyllysine antibody-based immunoseparation of acetylpeptides followed by nano-HPLC/MS/MS analysis, we identified 332 unique lysine-acetylated sites on 185 proteins. These proteins are mainly involved in cellular housekeeping functions such as central metabolism and protein synthesis. Fifity-nine of the lysine-acetylated proteins showed homology with lysine-acetylated proteins previously identified in E. coli, suggesting that acetylated proteins are more conserved. Notably, acetylation was found at or near the active sites predicted by Prosite signature, including SdhA, RocA, Kbl, YwjH, and YfmT, indicating that lysine acetylation may affect their activities. In 2-amino-3-ketobutyrate CoA ligase Kbl, a class II aminotransferase, a lysine residue involved in pyridoxal phosphate attachment was found to be acetylated. This data set provides evidence for the generality of lysine acetylation in eubacteria and opens opportunities to explore the consequences of acetylation modification on the molecular physiology of B. subtilis.

ISSN 

1615-9853

Link 

http://dx.doi.org/10.1002/pmic.201200001

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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