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.

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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