ArticleJournal of proteome research2018
Quantitative N-Terminal Footprinting of Pathogenic Mycobacteria Reveals Differential Protein Acetylation.
Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Advances in Decoding Bacterial N-Terminal Proteoforms: Technologies, Challenges, and Functional Insights.Microorganisms · 2026Review
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The regulatory functions of ESX-1 substrates, EspE and EspF, are separable from secretion.Journal of bacteriology · 2024Article
- N-terminal proteomics ofMicrobiology resource announcements · 2024Article
- The physiological effect of rimI/rimJ silencing by CRISPR interference in Mycobacterium smegmatis mcArchives of microbiology · 2023Article
- An N-acetyltransferase required for EsxA N-terminal protein acetylation and virulence in Mycobacterium marinum.bioRxiv : the preprint server for biology · 2023Article
- Miniprep assisted proteomics (MAP) for rapid proteomics sample preparation.Analytical methods : advancing methods and applications · 2023Article
- A Strong Cation Exchange Chromatography Protocol for Examining N-Terminal Proteoforms.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Protein N-terminal acylation: An emerging field in bacterial cell physiology.Current trends in microbiology · 2022Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- The genetic proteome: Using genetics to inform the proteome of mycobacterial pathogens.PLoS pathogens · 2021Review
- Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A New ESX-1 Substrate in Mycobacterium marinum That Is Required for Hemolysis but Not Host Cell Lysis.Journal of bacteriology · 2019Article
- Identification of N-terminal protein processing sites by chemical labeling mass spectrometry.Rapid communications in mass spectrometry : RCM · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
N-terminal acetylation (NTA) is a post-transcriptional modification of proteins that is conserved from bacteria to humans. In bacteria, the enzymes that mediate protein NTA also promote antimicrobial resistance. In pathogenic mycobacteria, which cause human tuberculosis and other chronic infections, NTA has been linked to pathogenesis and stress response, yet the fundamental biology underlying NTA of mycobacterial proteins remains unclear. We enriched, defined, and quantified the NT-acetylated populations of both cell-associated and secreted proteins from both the human pathogen, Mycobacterium tuberculosis, and the nontuberculous opportunistic pathogen, Mycobacterium marinum. We used a parallel N-terminal enrichment strategy from proteolytic digests coupled to charge-based selection and stable isotope ratio mass spectrometry. We show that NTA of the mycobacterial proteome is abundant, diverse, and primarily on Thr residues, which is unique compared with other bacteria. We isolated both the acetylated and unacetylated forms of 256 proteins, indicating that NTA of mycobacterial proteins is homeostatic. We identified 16 mycobacterial proteins with differential levels of NTA on the cytoplasmic and secreted forms, linking protein modification and localization. Our findings reveal novel biology underlying the NTA of mycobacterial proteins, which may provide a basis to understand NTA in mycobacterial physiology, pathogenesis, and antimicrobial resistance.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.