N-terminal proteomics of <i>Mycobacterium marinum</i> using bottom-up label-free quantitative analysis in data-dependent acquisition mode on a timsTOF Pro mass spectrometer
Daniel D. Hu, Simon D. Weaver, Owen A. Collars, Patricia A. Champion, Matthew M. Champion
Microbiology Resource Announcements · 2024-03
Abstract
ABSTRACT 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.
MeSH terms
- Proteomics
- Acetyltransferase
- Proteome
- Acetylation
- Mycobacterium tuberculosis
- Mass spectrometry
- Virulence
- Mycobacterium marinum
- Biology
- Computational biology
- Chemistry
- Microbiology
- Mycobacterium