N-terminal proteomics of Mycobacterium marinum using bottom-up label-free quantitative analysis in data-dependent acquisition mode on a timsTOF Pro mass spectrometer.
Daniel D HuSimon D WeaverOwen A CollarsPatricia A ChampionMatthew M ChampionPublished in: Microbiology resource announcements (2024)
N-terminal acetylation in Mycobacterium tuberculosis is correlated with pathogenic activity. We used genomics and bottom-up proteomics to identify protein Emp1 as the sole acetyltransferase responsible for acetylation of EsxA, a known virulence factor. Using custom data analysis, we screened the proteome to identify 22 additional putative substrates of Emp1.
Keyphrases
- label free
- data analysis
- mycobacterium tuberculosis
- escherichia coli
- pulmonary tuberculosis
- pseudomonas aeruginosa
- histone deacetylase
- high resolution
- staphylococcus aureus
- biofilm formation
- mass spectrometry
- protein protein
- amino acid
- electronic health record
- big data
- binding protein
- cystic fibrosis
- machine learning
- small molecule
- artificial intelligence
- candida albicans