Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli

High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans

“…Further studies of the Ser/Thr phosphorylation system will deepen our understanding of the physiology and pathogenesis of L. interrogans. Like phosphorylation, there are also differences in the acetylation systems between L. interrogans and E. coli, including the consensus sequences flanking the acetylation sites and the overrepresented functional classes [26]. Previous studies in E. coli and Salmonella enterica have proposed a Glx methylation consensus sequence, Glx-Glx-X-X-A-S/T, and methylation occurred strictly at the second Glx residue [43].…”

“…In particular, phosphorylation, acetylation and methylation, which are the most extensively studied PTMs, are all acknowledged to be important for regulating protein activities [21][22][23]. Recently, the analysis of phosphorylation at Ser/Thr/Tyr residues in the model bacteria Bacillus subtilis and Escherichia coli, and the analysis of acetylation at Lys residue in E. coli were accomplished by taking advantage of the modified peptide enrichment techniques [24][25][26]. A variety of phosphoproteins and acetylproteins were found to be involved in metabolic processes.…”

Succinylome Analysis Reveals the Involvement of Lysine Succinylation in Metabolism in Pathogenic Mycobacterium tuberculosis*

“…Among the hundreds of different PTMs, acylations at lysine residues, such as acetylation (3)(4)(5)(6), malonylation (7,8), crotonylation (9,10), propionylation (11)(12)(13), butyrylation (11,13), and succinylation (7, 14 -16) are crucial for functional regulations of many prokaryotic and eukaryotic proteins. Because these lysine PTMs depend on the acyl-CoA metabolic intermediates, such as acetyl-CoA (Ac-CoA), succinyl-CoA, and malonylCoA, lysine acylation could provide a mechanism to respond to changes in the energy status of the cell and regulate energy metabolism and the key metabolic pathways in diverse organisms (17,18).…”

Proteomic analysis of post translational modifications in cyanobacteria

“…The first system-wide study of bacterial acetylome was conducted in Escherichia coli, by employing lysine-acetylated peptide immunoprecipitation and LC-MS/MS [80,81]. Then this approach has become a standard procedure in bacterial acetylome analyses [79][80][81][82].…”

“…The first system-wide study of bacterial acetylome was conducted in Escherichia coli, by employing lysine-acetylated peptide immunoprecipitation and LC-MS/MS [80,81]. Then this approach has become a standard procedure in bacterial acetylome analyses [79][80][81][82]. Our group provides the first extensive data on lysine acetylation in cyanobacterium Synechocystis 6803 based on this method, which is also the first study of protein lysine acetylation reported in cyanobacteria [23].…”