Comprehensive profiling of lysine acetylome in Staphylococcus aureus

The Gram-positive bacterium Staphylococcus aureus ( S. aureus ) is a wide spread common opportunistic pathogen that causes a wide variety of infectious diseases, from benign skin infections to life-threatening diseases such as the methicillin-resistant Staphylococcus aureus (MRSA) infection. Although emerging evidence suggests that lysine acetylation may play critical roles in bacterial physiology, the atlas of acetylome in S. aureus has not been studied. To comprehensively profile protein lysine acetylation in S. aureus , we used an integrated approach that combined immune affinity peptide enrichment using anti-lysine acetylation antibody, high-pH HPLC fractionation, and HPLC/mass spectrometry analysis. This study led to the identification of 1361 non-redundant acetylation sites on 412 proteins found in a search of S. aureus protein database extracted from the Swiss-Prot database. We further performed bioinformatic analysis to characterize this modification, including gene ontology annotation, protein-protein interaction, and domain analysis of the acetylation sites. We found that the acetylated proteins were enriched in multiple biological pathways, such as ribosomal function and energy metabolism. Our data provides a rich source for functional studies of lysine acetylation in S. aureus .