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.

中文翻译：

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铜绿假单胞菌的赖氨酸琥珀酰化和乙酰化

铜绿假单胞菌（Pseudomonas aeruginosa）是一种多药耐药的人机会病原体，主要参与医院感染。不幸的是，缺乏有效的抗菌剂。在翻译后修饰（PTM）水平上探索其生理学可能有助于更新战斗策略。最近，在细菌中发现了赖氨酸琥珀酰化，这似乎是一个有趣的PTM。我们介绍了铜绿假单胞菌的第一个琥珀酰基和乙酰基使用二维免疫亲和方法与纳米液相色谱串联质谱联用，在四种不同碳源存在下培养PA14。共鉴定了1520个琥珀酰化（612个蛋白）和1102个乙酰化（522个蛋白）赖氨酸残基。柠檬酸盐是碳源，我们在其中鉴定出更多的修饰蛋白。有趣的是，观察到有622个赖氨酸残基（312个蛋白）被乙酰化或琥珀酰化。这些蛋白质中的一些与毒力，适应性，抗性等有关。无标记的定量指出了相同蛋白质（未修饰，琥珀酰化或乙酰化）存在不同蛋白质形式，并暗示了碳源不同的丰度。铜绿假单胞菌。