Malonyl-proteome profiles of Staphylococcus aureus reveal lysine malonylation modification in enzymes involved in energy metabolism

Abstract Background Protein lysine malonylation, a novel post-translational modification (PTM), has been recently linked with energy metabolism in bacteria. Staphylococcus aureus is the third most important foodborne pathogen worldwide. Nonetheless, substrates and biological roles of malonylation are still poorly understood this pathogen. Results Using anti-malonyl-lysine antibody enrichment high-resolution LC-MS/MS analysis, 440 lysine-malonylated sites were identified 281 proteins S. strain. The frequency valine position ? 1 alanine at + 2 4 positions was high. KEGG pathway analysis showed that six categories highly enriched, including ribosome, glycolysis/gluconeogenesis, pentose phosphate (PPP), tricarboxylic acid cycle (TCA), valine, leucine, isoleucine degradation, aminoacyl-tRNA biosynthesis. In total, 31 malonylated shared homology previously E. coli, indicating conserved among Key rate-limiting enzymes central carbon metabolic pathways also found to be , namely pyruvate kinase (PYK), 6-phosphofructokinase, phosphoglycerate kinase, dihydrolipoyl dehydrogenase, F1F0-ATP synthase. Notably, or near protein active sites, KH domain protein, thioredoxin, dehydrogenase (ALD), (LpdA), oxidase CidC, catabolite control A (CcpA), thus suggesting may affect activity such enzymes. Conclusions Data presented herein expand current knowledge on prokaryotes indicate potential bacterial physiology metabolism.