Global lysine acetylation in Escherichia coli results from growth conditions that favor acetate fermentation

Abstract

Conclusion.We profiled protein acetylation in E. coli during growth on glucose and xylose 126 at both high and low sugar concentrations. We did not observe major differences amongst the 127 lysines acetylated during respective growth on these two sugars. Rather, the observed changes 128 7 in lysine acetylation were principally correlated with the initial sugar concentration, with higher 129 sugar concentrations causing more acetylation. These results indicate that acetylation is 130 agnostic to the metabolic route and simply targets accessible lysines, which may or may not 131 alter enzyme activity. They further support the hypothesis that lysine acetylation results from the 132 buildup of metabolic intermediates, principally acetyl phosphate, under conditions that favor 133 acetate production (Figure S1). 134 135 ACKNOWLEDGMENT 136

Genome- and Proteome-Wide Analysis of Lysine Acetylation in Vibrio vulnificus Vv180806 Reveals Its Regulatory Roles in Virulence and Antibiotic Resistance

“…The KEGG pathway enrichment analysis of acetylated proteins revealed the overrepresentation of central metabolic pathways, including citric acid (TCA) cycle, purine metabolism, and pyrimidine metabolism ( Figure 5D). This observation is in accord with those in other organisms and reflects a regulatory role of acetylation in central metabolism (Xie et al, 2016a;Schilling et al, 2019). Notably, the enrichment of carbohydrate metabolism and energy metabolism pathways indicates that acetylated modification may play an important role in the carbon source utilization of this bacterial strain (Wang et al, 2010).…”

“…Recent developments in high resolution mass spectrometry and the advent of specific purification methods have allowed large-scale analyses of protein acetylation, and have provided valuable insights into protein regulation. To date, the proteome-wide lysine acetylation profiles have been analyzed for a number of eukaryotes and prokaryotes, including important bacterial pathogens such as Escherichia coli ( Zhang et al, 2009 , 2013 ; Schilling et al, 2019 ), Staphylococcus aureus ( Zhang et al, 2014 ), Vibrio parahaemolyticus ( Pan et al, 2014 ), Mycobacterium tuberculosis ( Xie et al, 2016b ), Vibrio cholerae ( Jers et al, 2017 ), Pseudomonas aeruginosa ( Gaviard et al, 2018 ), Salmonella enterica ( Li et al, 2018 ), and Streptococcus pneumoniae ( Liu et al, 2018 ). These studies implied that protein lysine acetylation might play important roles in bacterial pathogenesis and drug resistance ( Ren et al, 2017 ; Li et al, 2018 ).…”

Regulation of translation by lysine acetylation inEscherichia coli

“…The membrane was washed 4x with PBST for 5 minutes each and incubated for 1 hour in the dark at room temperature with anti-rabbit IgG HRP-linked secondary antibody (Cell Signaling, Danvers, MA) diluted 2000-fold in 5% milk. The membrane was washed 4x with PBST for 5 minutes each, incubated in ECL blotting substrate (Abcam) and imaged in the Protein Simple machine (Bio-Techne) (13, 19).…”

“…Proteins are principally acetylated when cells enter stationary phase during growth on excess carbon (7, 18, 19). To maintain flux through glycolysis, E. coli can ferment excess carbon to acetate through the Pta-AckA pathway, where phosphotransacetylase (Pta) converts acetyl-CoA and inorganic phosphate to acetyl phosphate and free CoA, and then acetate kinase (AckA) converts acetyl phosphate and ADP to acetate and ATP (20).…”

Carbon Metabolism and the ROS Scavenging System Participate in Nostoc flagelliforme’s Adaptive Response to Dehydration Conditions through Protein Acetylation

“…The differences in the LysAc motif in these organisms implicate the existence of different acyltransferases or deacylases in prokaryotes. In E. coli, glycine at the −1(log 2) position, alanine at the +1(log 2) position, and glutamic acid at the +5(log 2) position were overrepresented, 43 suggesting that acetylation of this protein might be important for its function.…”