赖氨酸
枯草芽孢杆菌
乙酰化
生物化学
生物
酰化
代谢途径
新陈代谢
氨基酸
化学
细菌
遗传学
基因
催化作用
作者
Mingya Zhang,TianXian Liu,Le Wang,Yuqi Huang,Rufeng Fan,Ke Ma,Yunbo Kan,Minjia Tan,Jun‐Yu Xu
标识
DOI:10.1016/j.jprot.2022.104767
摘要
Lysine acetylation is a common posttranslational modification that regulates numerous biochemical functions in both eukaryotic and prokaryotic species. In addition, several new non-acetyl acylations are structurally different from lysine acetylation and participate in diverse physiological functions. Here, a comprehensive analysis of several lysine acylomes was performed by combining the high-affinity antibody enrichment with high-resolution LC-MS/MS. In total, we identified 2536 lysine acetylated sites, 4723 propionylated sites, 2150 succinylated sites and 3001 malonylated sites in Bacillus subtilis, respectively. These acylated proteins account for 35.8% of total protein in this bacterium. The four lysine acylomes showed a motif preference for glutamate surrounding the modified lysine residues, and a functional preference for several metabolic pathways, such as carbon metabolism, fatty acid metabolism, and ribosome. In addition, more protein-protein interaction clusters were identified in the propionylated substrates than other three lysine acylomes. In summary, our study presents a global landscape of acylation in the Gram-positive model organism Bacillus and their potential functions in metabolism and physiology.
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