ArticleThe Journal of biological chemistry2014
Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Intracellular peroxynitrite perturbs redox balance, bioenergetics, and Fe-S cluster homeostasis in Mycobacterium tuberculosis.Redox biology · 2024Review
- Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021Review
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways inThe Journal of biological chemistry · 2020Article
- Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020Review
- Oxidative Stress-Generating Antimicrobials, a Novel Strategy to Overcome Antibacterial Resistance.Antioxidants (Basel, Switzerland) · 2020Review
- Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020Article
- Mycoredoxins Are Required for Redox Homeostasis and Intracellular Survival in the Actinobacterial PathogenAntioxidants (Basel, Switzerland) · 2019Article
- Kinetics of formation and reactivity of the persulfide in the one-cysteine peroxiredoxin fromThe Journal of biological chemistry · 2019Article
- The role of thiols in antioxidant systems.Free radical biology & medicine · 2019Review
- Reactive species and pathogen antioxidant networks during phagocytosis.The Journal of experimental medicine · 2019Review
- Mycobacterium tuberculosis WhiB3 maintains redox homeostasis and survival in response to reactive oxygen and nitrogen species.Free radical biology & medicine · 2019Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
- Stable integration of the Mrx1-roGFP2 biosensor to monitor dynamic changes of the mycothiol redox potential in Corynebacterium glutamicum.Redox biology · 2019Article
- A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress.PloS one · 2018Article
- European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).Redox biology · 2017Review
- The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response ofThe Journal of biological chemistry · 2017Article
- The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress.Scientific reports · 2017Article
- WhiB4 Regulates the PE/PPE Gene Family and is Essential for Virulence of Mycobacterium marinum.Scientific reports · 2017Article
- Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress.Scientific reports · 2017Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis (M. tuberculosis), the pathogen responsible for tuberculosis, detoxifies cytotoxic peroxides produced by activated macrophages. M. tuberculosis expresses alkyl hydroxyperoxide reductase E (AhpE), among other peroxiredoxins. So far the system that reduces AhpE was not known. We identified M. tuberculosis mycoredoxin-1 (MtMrx1) acting in combination with mycothiol and mycothiol disulfide reductase (MR), as a biologically relevant reducing system for MtAhpE. MtMrx1, a glutaredoxin-like, mycothiol-dependent oxidoreductase, directly reduces the oxidized form of MtAhpE, through a protein mixed disulfide with the N-terminal cysteine of MtMrx1 and the sulfenic acid derivative of the peroxidatic cysteine of MtAhpE. This disulfide is then reduced by the C-terminal cysteine in MtMrx1. Accordingly, MtAhpE catalyzes the oxidation of wt MtMrx1 by hydrogen peroxide but not of MtMrx1 lacking the C-terminal cysteine, confirming a dithiolic mechanism. Alternatively, oxidized MtAhpE forms a mixed disulfide with mycothiol, which in turn is reduced by MtMrx1 using a monothiolic mechanism. We demonstrated the H2O2-dependent NADPH oxidation catalyzed by MtAhpE in the presence of MR, Mrx1, and mycothiol. Disulfide formation involving mycothiol probably competes with the direct reduction by MtMrx1 in aqueous intracellular media, where mycothiol is present at millimolar concentrations. However, MtAhpE was found to be associated with the membrane fraction, and since mycothiol is hydrophilic, direct reduction by MtMrx1 might be favored. The results reported herein allow the rationalization of peroxide detoxification actions inferred for mycothiol, and more recently, for Mrx1 in cellular systems. We report the first molecular link between a thiol-dependent peroxidase and the mycothiol/Mrx1 pathway in Mycobacteria.
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