ArticleMolecular & cellular proteomics : MCP2014
Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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83 citing papers in PubMed, 155 citations in OpenAlex.
- An adenylyl cyclase switch reroutes carbon from growth to virulence lipids inbioRxiv : the preprint server for biology · 2026Article
- Acetylome Analysis inPathogens (Basel, Switzerland) · 2026Article
- Nicotinamide attenuates the virulence of colorectal cancer-associatedInfection and immunity · 2026Article
- Lysine acetylome profiling reveals a dual regulatory role in carbon flux redirection and RNA degradation inhibition inFrontiers in microbiology · 2026Article
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Metabolite dynamics over the course of anti-tuberculosis treatment in individuals with mild and severe tuberculosis.PLOS global public health · 2025Article
- Sirtuin inhibitors reduce intracellular growth of M. tuberculosis in human macrophages via modulation of host cell immunity.Scientific reports · 2024Article
- Facile metabolic reprogramming distinguishes mycobacterial adaptation to hypoxia and starvation: ketosis drives starvation-induced persistence in M. bovis BCG.Communications biology · 2024Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
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- Acetylomics reveals an extensive acetylation diversity withinmicroLife · 2024Article
- An insight into the role of the N-terminal domain ofFrontiers in molecular biosciences · 2024Article
- Comparative Lysine Acetylome Analysis of Y. pestis YfiQ/CobB Mutants Reveals that Acetylation of SlyA Lys73 Significantly Promotes Biofilm Formation of Y. pestis.Microbiology spectrum · 2023Article
- Systematic Analysis of Lysine Acetylation Reveals Diverse Functions in Azorhizobium caulinodans Strain ORS571.Microbiology spectrum · 2023Article
- Holistic analysis of lysine acetylation in aquaculture pathogenic bacteriaFrontiers in veterinary science · 2023Article
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- Acetylation of Lactate Dehydrogenase Negatively Regulates the Acidogenicity of Streptococcus mutans.mBio · 2022Article
- Cross-Talk of Protein Expression and Lysine Acetylation in Response to TMV Infection inACS omega · 2022Article
- Lysine Acylation Modification Landscape ofFrontiers in cell and developmental biology · 2022Article
- Propionylation of lysine, a new mechanism of short-chain fatty acids affecting bacterial virulence.American journal of translational research · 2022Review
23 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysine acetylation of proteins is a reversible post-translational modification that plays a critical regulatory role in both eukaryotes and prokaryotes. Mycobacterium tuberculosis is a facultative intracellular pathogen and the causative agent of tuberculosis. Increasing evidence shows that lysine acetylation may play an important role in the pathogenesis of M. tuberculosis. However, only a few acetylated proteins of M. tuberculosis are known, presenting a major obstacle to understanding the functional roles of reversible lysine acetylation in this pathogen. We performed a global acetylome analysis of M. tuberculosis H37Ra by combining protein/peptide prefractionation, antibody enrichment, and LC-MS/MS. In total, we identified 226 acetylation sites in 137 proteins of M. tuberculosis H37Ra. The identified acetylated proteins were functionally categorized into an interaction map and shown to be involved in various biological processes. Consistent with previous reports, a large proportion of the acetylation sites were present on proteins involved in glycolysis/gluconeogenesis, the citrate cycle, and fatty acid metabolism. A NAD(+)-dependent deacetylase (MRA_1161) deletion mutant of M. tuberculosis H37Ra was constructed and its characterization showed a different colony morphology, reduced biofilm formation, and increased tolerance of heat stress. Interestingly, lysine acetylation was found, for the first time, to block the immunogenicity of a peptide derived from a known immunogen, HspX, suggesting that lysine acetylation plays a regulatory role in immunogenicity. Our data provide the first global survey of lysine acetylation in M. tuberculosis. The dataset should be an important resource for the functional analysis of lysine acetylation in M. tuberculosis and facilitate the clarification of the entire metabolic networks of this life-threatening pathogen.
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