Abstract
Protein lysine acetylation is an evolutionarily conserved post-translational modification (PTM), which is dynamic and reversible, playing a crucial regulatory role in almost every aspect of metabolism, of both eukaryotes and prokaryotes. Several global lysine acetylome studies have been carried out in various bacteria, but thus far, there have been no reports of lysine acetylation for the commercially important aquatic animal pathogen Vibrio mimicus. In the present study, we used anti-Ac-K antibody beads to highly sensitive immune-affinity purification and combined high-resolution LC-MS/MS to perform the first global lysine acetylome analysis in V. mimicus, leading to the identification of 1,097 lysine-acetylated sites on 582 proteins, and more than half (58.4%) of the acetylated proteins had only one site. The analysis of acetylated modified peptide motifs revealed six significantly enriched motifs, namely, KacL, KacR, L(-2) KacL, LKacK, L(-7) EKac, and IEKac. In addition, bioinformatic assessments state clearly that acetylated proteins have a hand in many important biological processes in V. mimicus, such as purine metabolism, ribosome, pyruvate metabolism, glycolysis/gluconeogenesis, the TCA cycle, and so on. Moreover, 13 acetylated proteins were related to the virulence of V. mimicus. To sum up, this is a comprehensive analysis whole situation protein lysine acetylome in V. mimicus and provides an important foundation for in-depth study of the biological function of lysine acetylation in V. mimicus.
Highlights
Post-translational modification (PTM) of proteins is a significant regulatory mechanism that affects processes beyond gene expression in bacteria
Compared with the bacterial acetylomes of other fish pathogens studied, the proportion of acetylation proteins in this bacterium is lower than Vibrio alginolyticus (27.1%) and Aeromonas hydrophila (21.7%) (Pang et al, 2019; Sun et al, 2019), but is higher than Vibrio parahemolyticus (13.6%) (Pan et al, 2014)
We evaluated the distribution of lysine acetylated sites and showed that most proteins were single acetylation sites (58.4%), and more than five acetylated sites accounted for 6% (Figure 1B)
Summary
Post-translational modification (PTM) of proteins is a significant regulatory mechanism that affects processes beyond gene expression in bacteria. In recent years, accumulating evidence indicates that PTMs play a critical role in various physiological processes, such as immunometabolism (Diskin et al, 2020), protein synthesis and turnover (Rioseras et al, 2018), protein stability (Ishigaki et al, 2017; Sang et al, 2017), dormancy (Yang et al, 2018), nitrogen metabolism (Macek et al, 2019), and virulence (Xie et al, 2019). Among the hundreds of diverse PTMs, protein phosphorylation, acetylation, succinylation, pupylation and ubiquitin-like modifications, glycosylation, and lipidation play a major role in regulating bacterial cell cycle, cell metabolism, persistence, and virulence (Ren et al, 2016, 2019; Macek et al, 2019). Acetylation modification occurs on enzymes in several central metabolic processes of bacteria, such as tricarboxylic acid cycle, glycolysis/gluconeogenesis, and pyruvate metabolism (Li W.X. et al, 2020)
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