The acetylproteome of Gram-positive model bacterium Bacillus subtilis

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dc.contributor.authorDoo-Il Kim-
dc.contributor.authorB J Yu-
dc.contributor.authorJung-Ae Kim-
dc.contributor.authorY J Lee-
dc.contributor.authorSoo Keun Choi-
dc.contributor.authorSunghyun Kang-
dc.contributor.authorJae Gu Pan-
dc.date.accessioned2017-04-19T09:40:20Z-
dc.date.available2017-04-19T09:40:20Z-
dc.date.issued2013-
dc.identifier.issn1615-9853-
dc.identifier.uri10.1002/pmic.201200001ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11358-
dc.description.abstractNε-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.-
dc.publisherWiley-
dc.titleThe acetylproteome of Gram-positive model bacterium Bacillus subtilis-
dc.title.alternativeThe acetylproteome of Gram-positive model bacterium Bacillus subtilis-
dc.typeArticle-
dc.citation.titleProteomics-
dc.citation.number10-
dc.citation.endPage1736-
dc.citation.startPage1726-
dc.citation.volume13-
dc.contributor.affiliatedAuthorDoo-Il Kim-
dc.contributor.affiliatedAuthorJung-Ae Kim-
dc.contributor.affiliatedAuthorSoo Keun Choi-
dc.contributor.affiliatedAuthorSunghyun Kang-
dc.contributor.affiliatedAuthorJae Gu Pan-
dc.contributor.alternativeName김두일-
dc.contributor.alternativeName유병조-
dc.contributor.alternativeName김정애-
dc.contributor.alternativeName이용직-
dc.contributor.alternativeName최수근-
dc.contributor.alternativeName강성현-
dc.contributor.alternativeName반재구-
dc.identifier.bibliographicCitationProteomics, vol. 13, no. 10, pp. 1726-1736-
dc.identifier.doi10.1002/pmic.201200001-
dc.subject.keywordAcetylation-
dc.subject.keywordBacillus subtilis-
dc.subject.keywordBacteria-
dc.subject.keywordEnzymes-
dc.subject.keywordPTM-
dc.subject.localacetylation-
dc.subject.localAcetylation-
dc.subject.localBacillus subtilis-
dc.subject.localbacillus subtilis-
dc.subject.localbacteria-
dc.subject.localBacteria-
dc.subject.localbacteria (microorganisms)-
dc.subject.localenzyme-
dc.subject.localEnzymes-
dc.subject.localEnzyme-
dc.subject.localenzymes-
dc.subject.localPTM-
dc.subject.localPTMs-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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