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Updated: Feb 10, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Lysine Succinylation and Acetylation in Pseudomonas aeruginosa
Charlotte Gaviard1,2, Isabelle Broutin3, Pascal Cosette1,2
1Normandie Univ, UNIROUEN, INSA Rouen, CNRS, PBS , 76000 Rouen , France.
Abstract:
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 four different carbon sources using a 2D immunoaffinity approach coupled to nanoliquid chromatography tandem mass spectrometry. A total of 1520 succinylated (612 proteins) and 1102 acetylated (522 proteins) lysine residues were characterized. Citrate was the carbon source in which we identified the higher number of modified proteins. Interestingly, 622 lysine residues (312 proteins) were observed either acetylated or succinylated. Some of these proteins, were involved in virulence, adaptation, resistance, and so on. A label-free quantification points out the existence of different protein forms for a same protein (unmodified, succinylated or acetylated) and suggests different abundance as a function of the carbon sources. This work is a promising starting point for further investigations on the biological role of lysine succinylation in P. aeruginosa.
Insights
This study maps lysine succinylation and acetylation in Pseudomonas aeruginosa, revealing citrate as a key carbon source for these modifications. Understanding these post-translational modifications offers new avenues for combating drug-resistant bacteria.
Area of Science:
- Microbiology
- Biochemistry
- Proteomics
Background:
- Pseudomonas aeruginosa is a multi-drug-resistant pathogen causing significant nosocomial infections.
- Effective antibacterial strategies are limited, necessitating novel approaches.
- Post-translational modifications (PTMs) offer potential targets for new therapies.
Purpose of the Study:
- To characterize the succinylome and acetylome of P. aeruginosa PA14.
- To investigate the impact of different carbon sources on lysine succinylation and acetylation.
- To explore the potential of these PTMs in understanding bacterial physiology and developing new treatments.
Main Methods:
- Utilized a 2D immunoaffinity approach.
- Employed nanoliquid chromatography tandem mass spectrometry (nLC-MS/MS).
- Analyzed P. aeruginosa PA14 cultured with four distinct carbon sources.
Main Results:
- Identified 1520 succinylated and 1102 acetylated lysine residues across 612 and 522 proteins, respectively.
- Citrate supported the highest number of protein modifications.
- Discovered 622 dual-modified lysine residues (312 proteins) involved in virulence and resistance.
Conclusions:
- This research provides the first comprehensive succinylome and acetylome of P. aeruginosa.
- Lysine succinylation and acetylation are prevalent PTMs influenced by carbon source availability.
- Findings suggest these modifications play roles in bacterial adaptation and resistance, offering potential therapeutic targets.
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