2018 Volume 3 Issue 1 Pages 15-22
Post-translational modifications extend the varieties of chemical characteristics of fundamental 20 amino acid residues, and thereby enable proteins to function in diverse biological processes. Of the post-translational modifications, lysine acylations change the chemical properties of lysine residues through the transfer of acyl groups with the different charge states and bulkiness. Recent development of mass spectrometric technology discovered several lysine acylations. Furthermore, these acylations were identified on hundreds to thousands of proteins, suggesting complex system involved by lysine acylations. To understand fundamental and common functions by lysine acylations among organisms ranging from bacteria to human, we characterized lysine acylations such as acetylation, propionylation, and succinylation in bacteria. Here, we mainly described our studies on lysine propionylation and succinylation. We identified these lysine acylations on a proteome-wide scale in 5 bacterial species. Furthermore, by using protein tertiary structure information, we speculated the roles of dozens of lysine acylations. Interestingly, many acylation sites were located at the positions near the bound ligands. Comparison of the characteristics of these two types of acylation suggested their different roles in cellular processes. To evaluate which modification effects are different between propionylation and succinylation, we conducted in silico docking simulation analysis of unmodified, propionylated, and succinylated enzymes with its ligand. The result suggested that lysine propionylation and succinylation can have a moderate and strong influence on protein function, respectively.
