Available online 3 November 2022, 104767

Global landscape of lysine acetylome, propionylome, succinylome and malonylome in Bacillus subtilis.

The commonality of substrate features in the four lysine acylations.

Unique and specific pathway characterizations in each kind of lysine acylation.

The potential biological consequences of the substrate proteins shared by the four lysine acylations.

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.

Bacillus subtilis

Lysine acetylation

Lysine propionylation

Lysine succinylation

Lysine malonylation

Mass spectrometry

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