Comprehensive Profiling of Lysine Acetylome in Staphylococcus Aureus
Jul 20, 2014 Email"> PrintText Size
The Gram-positive bacterium Staphylococcus aureus (S. aureus) is a widely 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. aureushas not been studied.
To comprehensively profile protein lysine acetylation in S. aureus, scientists from Chemical Proteomics Center of Shanghai Institute of Materia Medica (SIMM) 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 1,361 non-redundant acetylation sites on 412 proteins found in a search of S. aureusprotein database extracted from the Swiss-Prot database. They further performed bioinformatic analysis to characterize this modification, including gene ontology annotation, protein-protein interaction, and domain analysis of the acetylation sites. The analysis result demonstrates that the acetylated proteins were mainly enriched in ribosome, which implies the vital roles of protein acetylation in regulating the biogenesis of proteins.
This study represented the largest lysine acetylome dataset for Gram-positive bacterium S. aureus, which greatly expanded the known lysine acetylation sites and acetylated proteins in Gram-positive bacteria. This dataset could serve as a rich source for the biology of protein acetylation and physiology in S. aureus. Given the fact that the HDAC inhibitor sodium butyrate can inhibit S. aureus internalization in bovine mammary epithelial cells, a lysine acetylation pathway may represent a new avenue for developing novel therapeutics to combat the menace of this nosocomial pathogen.
This work has been published on Science China Chemistry (2014, 57, 732-738).
The Gram-positive bacterium Staphylococcus aureus (S. aureus) is a widely 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. aureushas not been studied.
To comprehensively profile protein lysine acetylation in S. aureus, scientists from Chemical Proteomics Center of Shanghai Institute of Materia Medica (SIMM) 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 1,361 non-redundant acetylation sites on 412 proteins found in a search of S. aureusprotein database extracted from the Swiss-Prot database. They further performed bioinformatic analysis to characterize this modification, including gene ontology annotation, protein-protein interaction, and domain analysis of the acetylation sites. The analysis result demonstrates that the acetylated proteins were mainly enriched in ribosome, which implies the vital roles of protein acetylation in regulating the biogenesis of proteins.
This study represented the largest lysine acetylome dataset for Gram-positive bacterium S. aureus, which greatly expanded the known lysine acetylation sites and acetylated proteins in Gram-positive bacteria. This dataset could serve as a rich source for the biology of protein acetylation and physiology in S. aureus. Given the fact that the HDAC inhibitor sodium butyrate can inhibit S. aureus internalization in bovine mammary epithelial cells, a lysine acetylation pathway may represent a new avenue for developing novel therapeutics to combat the menace of this nosocomial pathogen.
This work has been published on Science China Chemistry (2014, 57, 732-738).
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