Lozano-Terol Gema, Chiozzi Riccardo Zenezini, Gallego-Jara Julia, Sola-Martínez Rosa Alba, Vivancos Adrián Martínez, Ortega Álvaro, Heck Albert J R, Díaz Manuel Cánovas, de Diego Puente Teresa
Department of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", 30100 Murcia, Spain.
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, Utrecht 3584 CH, the Netherlands.
iScience. 2024 Jan 24;27(2):109017. doi: 10.1016/j.isci.2024.109017. eCollection 2024 Feb 16.
Nε-lysine acetylation is a common posttranslational modification observed in . In the present study, integrative analysis of the proteome and acetylome was performed using label-free quantitative mass spectrometry to analyze the relative influence of three factors affecting growth. The results revealed differences in the proteome, mainly owing to the type of culture medium used (defined or complex). In the acetylome, 7482 unique acetylation sites were identified. Acetylation is directly related to the abundance of proteins, and the level of acetylation in each type of culture is associated with extracellular acetate concentration. Furthermore, most acetylated lysines in the exponential phase remained in the stationary phase without dynamic turnover. Interestingly, unique acetylation sites were detected in proteins whose presence or abundance was linked to the type of culture medium. Finally, the biological function of the acetylation changes was demonstrated for three central metabolic proteins (GapA, Mdh, and AceA).
Nε-赖氨酸乙酰化是一种常见的翻译后修饰。在本研究中,使用无标记定量质谱法对蛋白质组和乙酰化蛋白质组进行综合分析,以分析影响生长的三个因素的相对影响。结果显示蛋白质组存在差异,主要归因于所用培养基的类型(限定培养基或复杂培养基)。在乙酰化蛋白质组中,鉴定出7482个独特的乙酰化位点。乙酰化与蛋白质丰度直接相关,每种培养类型中的乙酰化水平与细胞外乙酸盐浓度相关。此外,指数生长期的大多数乙酰化赖氨酸在稳定期保持不变,没有动态转换。有趣的是,在其存在或丰度与培养基类型相关的蛋白质中检测到独特的乙酰化位点。最后,对三种核心代谢蛋白(GapA、Mdh和AceA)的乙酰化变化的生物学功能进行了验证。