title: The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
abstract: N(ε) -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.
authors.affiliation: Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Korea.
authors.forename: Dooil
authors.initials: D
authors.lastname: Kim
authors.forename: Byung Jo
authors.initials: BJ
authors.lastname: Yu
authors.forename: Jung Ae
authors.initials: JA
authors.lastname: Kim
authors.forename: Yong-Jik
authors.initials: YJ
authors.lastname: Lee
authors.forename: Soo-Geun
authors.initials: SG
authors.lastname: Choi
authors.forename: Sunghyun
authors.initials: S
authors.lastname: Kang
authors.forename: Jae-Gu
authors.initials: JG
authors.lastname: Pan
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D020134:Catalytic Domain; D002851:Chromatography, High Pressure Liquid; D016384:Consensus Sequence; D047468:Immunoprecipitation; D058977:Molecular Sequence Annotation; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
chemical_list: D001426:Bacterial Proteins; D010750:Phosphoproteins; D020543:Proteome; D000123:Acetyltransferases; C020679:glycine acetyltransferase