ArticleScientific reports2017
AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Regulating microbial cell factories to resist ROS stress in chemical production.Archives of microbiology · 2026Review
- Membrane-associated effluxosomes coordinate multi-metal resistance in Mycobacterium tuberculosis.The EMBO journal · 2026Article
- Role of thioredoxin reductase (TrxB) in oxidative stress response ofJournal of bacteriology · 2025Article
- Insights into Active Site Cysteine Residues inInternational journal of molecular sciences · 2025Review
- Multivariable regression models improve accuracy and sensitive grading of antibiotic resistance mutations in Mycobacterium tuberculosis.Nature communications · 2025Article
- Altering the redox status ofeLife · 2025Article
- Host- and Age-Dependent Transcriptional Changes inInternational journal of molecular sciences · 2022Article
- Multi-Omics Profiling Specifies Involvement of Alternative Ribosomal Proteins in Response to Zinc Limitation inFrontiers in microbiology · 2022Article
- Recombinant AhpC antigen fromTurkish journal of biology = Turk biyoloji dergisi · 2022Article
- From infection niche to therapeutic target: the intracellular lifestyle ofMicrobiology (Reading, England) · 2021Review
- Genome analyses of 174 strains ofMicrobial genomics · 2021Article
- Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways inThe Journal of biological chemistry · 2020Article
- Structure-function analyses of alkylhydroperoxidase D fromThe Journal of biological chemistry · 2020Article
- Reactive species and pathogen antioxidant networks during phagocytosis.The Journal of experimental medicine · 2019Review
- Molecular Mechanisms of AhpC in Resistance to Oxidative Stress inFrontiers in microbiology · 2019Article
- Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions.Scientific reports · 2018Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the highly oxidative environment of the phagosomal lumen, the need for maintaining redox homeostasis is a critical aspect of mycobacterial biology. The pathogens are equipped with the sophisticated thioredoxin- (Trx) and peroxiredoxin system, including TrxC and the alkyl hydroperoxide reductase subunit C (AhpC), whereby TrxC is one of the reducing partners of AhpC. Here we visualize the redox modulated dodecamer ring formation of AhpC from Mycobacterium bovis (BCG strain; MbAhpC) using electron microscopy and present novel insights into the unique N-terminal epitope (40 residues) of mycobacterial AhpC. Truncations and amino acid substitutions of residues in the unique N-terminus of MbAhpC provide insights into their structural and enzymatic roles, and into the evolutionary divergence of mycobacterial AhpC versus that of other bacteria. These structural details shed light on the epitopes and residues of TrxC which contributes to its interaction with AhpC. Since human cells lack AhpC, the unique N-terminal epitope of mycobacterial AhpC as well as the MbAhpC-TrxC interface represent an ideal drug target.
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