Nalpas Nicolas, Kentache Takfarinas, Dé Emmanuelle, Hardouin Julie
INSA Rouen Normandie, CNRS, Polymers, Biopolymers, Surfaces Laboratory UMR 6270, University of Rouen Normandie, Rouen F-76000, France.
INSERM US 51, CNRS UAR 2026, HeRacLeS-PISSARO, Normandie Université, University of Rouen Normandie, Rouen F-76000, France.
J Proteome Res. 2023 Jul 7;22(7):2339-2351. doi: 10.1021/acs.jproteome.3c00097. Epub 2023 May 25.
Over the past 30 years, has been described as an important nosocomial pathogen due to frequent ventilator-associated infections. Many biological processes of remain elusive, such as the formation of an air-liquid biofilm (pellicle). Several studies demonstrated the importance of post-translational modifications (PTMs) in physiology. Here, we investigated K-trimethylation in ATCC 17978 in planktonic and pellicle modes using proteomic analysis. To identify the most high-confidence K-trimethylated peptides, we compared different sample preparation methods (i.e., strong cation exchange, antibody-capture) and processing software (i.e., different database search engines). We identified, for the first time, 84 K-trimethylated proteins, many of which are involved in DNA and protein synthesis (HupB, RplK), transporters (Ata, AdeB), or lipid metabolism processes (FadB, FadD). In comparison with previous studies, several identical lysine residues were observed acetylated or trimethylated, indicating the presence of proteoforms and potential PTM cross-talks. This is the first large-scale proteomic study of trimethylation in and will be an important resource for the scientific community (availability in Pride repository under accession PXD035239).
在过去30年里，由于频繁引发呼吸机相关性感染，[病原体名称未给出]已被描述为一种重要的医院病原体。[病原体名称未给出]的许多生物学过程仍不清楚，比如气液生物膜（菌膜）的形成。多项研究证明了翻译后修饰（PTMs）在[病原体名称未给出]生理学中的重要性。在此，我们使用蛋白质组学分析，研究了[病原体名称未给出]ATCC 17978在浮游和菌膜模式下的赖氨酸三甲基化情况。为了鉴定出最具可信度的赖氨酸三甲基化肽段，我们比较了不同的样品制备方法（即强阳离子交换、抗体捕获）和处理软件（即不同的数据库搜索引擎）。我们首次鉴定出84种赖氨酸三甲基化蛋白，其中许多蛋白参与DNA和蛋白质合成（HupB、RplK）、转运蛋白（Ata、AdeB）或脂质代谢过程（FadB、FadD）。与之前的研究相比，观察到几个相同的赖氨酸残基发生了乙酰化或三甲基化，这表明存在蛋白质异构体和潜在的翻译后修饰相互作用。这是首次对[病原体名称未给出]的三甲基化进行大规模蛋白质组学研究，将成为科学界的重要资源（可在Pride数据库中获取，登录号为PXD035239）。
