ArticleJournal of bacteriology2011
Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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Who cites it
41 citing papers in PubMed, 79 citations in OpenAlex.
- Metabolomics profiling reveals changes in peptidoglycan and redox metabolism between ancient and modernMicrobiology spectrum · 2026Article
- Host oxidative stress primes mycobacteria for rapid antibiotic resistance evolution.Nature communications · 2026Article
- Ecological and genetic regulation of nutritional composition, pasting properties and metabolomic profiles in foxtail millet.Food chemistry: X · 2026Article
- Host oxidative stress primes mycobacteria for rapid antibiotic resistance evolution.Research square · 2025Article
- Article
- Ergothioneine, Ovothiol A, and Selenoneine-Histidine-Derived, Biologically Significant, Trace Global Alkaloids.Molecules (Basel, Switzerland) · 2022Review
- From infection niche to therapeutic target: the intracellular lifestyle ofMicrobiology (Reading, England) · 2021Review
- PmtA Regulates Pyocyanin Expression and Biofilm Formation inFrontiers in microbiology · 2021Article
- The biology of ergothioneine, an antioxidant nutraceutical.Nutrition research reviews · 2020Review
- 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
- Engineering the YeastFrontiers in bioengineering and biotechnology · 2019Article
- Stable integration of the Mrx1-roGFP2 biosensor to monitor dynamic changes of the mycothiol redox potential in Corynebacterium glutamicum.Redox biology · 2019Article
- The functional interplay of low molecular weight thiols in Mycobacterium tuberculosis.Journal of biomedical science · 2018Article
- Host-pathogen redox dynamics modulate Mycobacterium tuberculosis pathogenesis.Pathogens and disease · 2018Article
- Pseudomonas aeruginosamSphere · 2018Article
- Compounds with Potential Activity against Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2018Article
- Role of Ergothioneine in Microbial Physiology and Pathogenesis.Antioxidants & redox signaling · 2018Review
- A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress.PloS one · 2018Article
- The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The mshA::Tn5 mutant of Mycobacterium smegmatis does not produce mycothiol (MSH) and was found to markedly overproduce both ergothioneine and an ~15-kDa protein determined to be organic hydroperoxide resistance protein (Ohr). An mshA(G32D) mutant lacking MSH overproduced ergothioneine but not Ohr. Comparison of the mutant phenotypes with those of the wild-type strain indicated the following: Ohr protects against organic hydroperoxide toxicity, whereas ergothioneine does not; an additional MSH-dependent organic hydroperoxide peroxidase exists; and elevated isoniazid resistance in the mutant is associated with both Ohr and the absence of MSH. Purified Ohr showed high activity with linoleic acid hydroperoxide, indicating lipid hydroperoxides as the likely physiologic targets. The reduction of oxidized Ohr by NADH was shown to be catalyzed by lipoamide dehydrogenase and either lipoamide or DlaT (SucB). Since free lipoamide and lipoic acid levels were shown to be undetectable in M. smegmatis, the bound lipoyl residues of DlaT are the likely source of the physiological dithiol reductant for Ohr. The pattern of occurrence of homologs of Ohr among bacteria suggests that the ohr gene has been distributed by lateral transfer. The finding of multiple Ohr homologs with various sequence identities in some bacterial genomes indicates that there may be multiple physiologic targets for Ohr proteins.
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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.