A5024906450- Peptidase Inhibition and Analysis
- Pneumocystis jirovecii pneumonia detection and treatment
- Biochemical and Molecular Research
- Enzyme Structure and Function
- Glycosylation and Glycoproteins Research
University of Notre Dame
2023-2024
ABSTRACT N-terminal protein acetylation is a ubiquitous post-translational modification that impacts diverse cellular processes in higher organisms. Bacterial proteins are also N-terminally acetylated, but the mechanisms and consequences of this bacteria poorly understood. The major virulence factor EsxA (ESAT-6, early secreted antigen, 6 kDa) was one first acetylated identified bacteria. conserved mycobacterial pathogens, including Mycobacterium tuberculosis marinum , non-tubercular species...
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 of EsxA, a known virulence factor. Using custom data analysis, we screened proteome 22 additional putative substrates Emp1.
N-terminal protein acetylation is a ubiquitous post-translational modification that broadly impacts diverse cellular processes in higher organisms. Bacterial proteins are also N-terminally acetylated, but the mechanisms and consequences of this bacteria poorly understood. We previously quantified widespread pathogenic mycobacteria (C. R. Thompson, M. Champion, P.A. J Proteome Res 17(9): 3246-3258, 2018, https:// doi: 10.1021/acs.jproteome.8b00373). The major virulence factor EsxA (ESAT-6,...