Dataset Information

Lysine succinylation and acetylation in Pseudomonas aeruginosa

ABSTRACT: The present data set provides the first description of lysine succinylation and lysine acetylation in P. aeruginosa grown in 4 carbon sources using a two-dimensional immunoaffinity approach coupled with nanoliquid chromatography tandem mass spectrometry. A total of 1522 succinylated sites (612 proteins) and 1103 acetylated sites (522 proteins) were characterized.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Pseudomonas Aeruginosa (strain Ucbpp-pa14)

SUBMITTER: Julie Hardouin

LAB HEAD: Julie HARDOUIN

PROVIDER: PXD008662 | Pride | 2018-05-21

REPOSITORIES: Pride

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Publications

Lysine Succinylation and Acetylation in Pseudomonas aeruginosa.

Gaviard Charlotte C Broutin Isabelle I Cosette Pascal P Dé Emmanuelle E Jouenne Thierry T Hardouin Julie J

Journal of proteome research 20180530 7

Pseudomonas aeruginosa is a multi-drug-resistant human opportunistic pathogen largely involved in nosocomial infections. Unfortunately, effective antibacterial agents are lacking. Exploring its physiology at the post-translational modifications (PTMs) level may contribute to the renewal of combat tactics. Recently, lysine succinylation was discovered in bacteria and seems to be an interesting PTM. We present the first succinylome and acetylome of P. aeruginosa PA14 cultured in the presence of fo ...[more]

PMID: 29770699

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Project description:Background: Lysine succinylation is a newly identified PTM, which exists widely from prokaryotes to eukaryotes and participates in various cellular processes, especially in the metabolic processes. Staphylococcus epidermidis is a commensal bacterium in the skin, which attracts more attention as a pathogen, especially in immunocompromised patients and neonates by attaching to medical devices and forming biofilms. However, the significance of lysine succinylation in proteins of Staphylococcus epidermidis has not been investigated. Materials and methods: Using antibody affinity enrichment followed by LC-MS/MS analysis, we examined the succinylome of Staphylococcus epidermidis (ATCC®12228™). Then, bioinformatics analysis was performed, including Gene Ontology, KEGG enrichment, motif characterization, secondary structure, protein-protein interaction, and BLAST analysis. Results: A total of 1557 succinylated lysine sites in 649 proteins were identified in Staphylococcus epidermidis (ATCC 12228). Among these succinylation proteins, GO annotation showed that proteins related to metabolic processes and binding activity accounted for the most based on the analysis of biological process and molecular function, respectively. KEGG pathway characterization indicated that proteins associated with the glycolysis/ gluconeogenesis, and citrate cycle (TCA cycle) pathway were more likely to be succinylated. Moreover, 13 conserved motifs were identified. The specific motif KsuD was conserved in model prokaryotes and eukaryotes. Succinylated proteins with this motif were highly enriched in the glycolysis/gluconeogenesis pathway. One succinylation site(K144) was identified in S-ribosylhomocysteine lyase, a key enzyme in the quorum sensing system, indicating the regulatory role succinylation may play in bacterial processes. Furthermore, 15 succinyltransferases and 18 desuccinylases(erasers) were predicted in S.epidermidis by BLAST analysis. Conclusions: We performed the first comprehensive profile of succinylation in Staphylococcus epidermidis and illustrated the significant role succinylation may play in energy metabolism, QS system, and other bacterial behaviors. This study may be a fundamental basis to investigate the underlying mechanisms of colonization, virulence, and infection of S. epidermidis, as well as provide a new insight into regulatory effects succinylation may lay on metabolic processes.

Dataset Information

Lysine succinylation and acetylation in Pseudomonas aeruginosa

Publications

Lysine Succinylation and Acetylation in Pseudomonas aeruginosa.

Similar Datasets

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