ArticleJournal of bacteriology1998
Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 159 citations in OpenAlex.
- Endogenous Expression of HSP70 and Thioredoxin-1 During Methamphetamine-Induced Degeneration.Biomedicines · 2026Article
- Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026Article
- Thioredoxin and its partner protein are essential for zoospore flagellar formation in Actinoplanes missouriensis.Communications biology · 2026Article
- Comparative genome analyses reveal insights into the marine adaptation of a novel bacterium Pontimicrobium maritimus sp. nov., isolated from seawater.Scientific reports · 2025Article
- Advancements in alternative approaches to address antimicrobial resistance in bacterial pneumonia: a comprehensive review.Frontiers in microbiology · 2025Review
- The multiplicity of thioredoxin systems meets the specific lifestyles of Clostridia.PLoS pathogens · 2024Article
- In Silico Safety Assessment ofInternational journal of molecular sciences · 2024Article
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- Gold complex compounds that inhibit drug-resistantFrontiers in antibiotics · 2023Article
- Evaluation of metal-based antimicrobial compounds for the treatment of bacterial pathogens.Journal of medical microbiology · 2021Review
- Comparison of Proteomic Responses as Global Approach to Antibiotic Mechanism of Action Elucidation.Antimicrobial agents and chemotherapy · 2020Article
- Oxidative Stress-Generating Antimicrobials, a Novel Strategy to Overcome Antibacterial Resistance.Antioxidants (Basel, Switzerland) · 2020Review
- Lactic Acid Fermentation ofFrontiers in microbiology · 2020Article
- Distinct Roles of Shewanella oneidensis Thioredoxin in Regulation of Cellular Responses to Hydrogen and Organic Peroxides.Applied and environmental microbiology · 2019Article
- Inactivation ofJournal of bacteriology · 2019Article
- Repurposing Auranofin, Ebselen, and PX-12 as Antimicrobial Agents Targeting the Thioredoxin System.Frontiers in microbiology · 2018Review
- Oxidative stress, protein damage and repair in bacteria.Nature reviews. Microbiology · 2017Review
- Development of ebsulfur analogues as potent antibacterials against methicillin-resistant Staphylococcus aureus.Bioorganic & medicinal chemistry · 2016Article
- Global Transcriptional Analysis of Virus-Host Interactions between Phage ϕ29 and Bacillus subtilis.Journal of virology · 2016Article
- Dimethyl sulfoxide reduction by a hyperhermophilic archaeon Thermococcus onnurineus NA1 via a cysteine-cystine redox shuttle.Journal of microbiology (Seoul, Korea) · 2016Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxin, a small, ubiquitous protein which participates in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, is an essential protein in Bacillus subtilis. A variety of stresses, including heat or salt stress or ethanol treatment, strongly enhanced the synthesis of thioredoxin in B. subtilis. The stress induction of the monocistronic trxA gene encoding thioredoxin occurs at two promoters. The general stress sigma factor, sigmaB, was required for the initiation of transcription at the upstream site, S(B), and the promoter preceding the downstream start site, S(A), was presumably recognized by the vegetative sigma factor, sigmaA. In contrast to the heat-inducible, sigmaA-dependent promoters preceding the chaperone-encoding operons groESL and dnaK, no CIRCE (for controlling inverted repeat of chaperone expression) was present in the vicinity of the start site, S(A). The induction patterns of the promoters differed, with the upstream promoter displaying the typical stress induction of sigmaB-dependent promoters. Transcription initiating at S(A), but not at S(B), was also induced after treatment with hydrogen peroxide or puromycin. Such a double control of stress induction at two different promoters seems to be typical of a subgroup of class III heat shock genes of B. subtilis, like clpC, and it either allows the cells to raise the level of the antioxidant thioredoxin after oxidative stress or allows stressed cells to accumulate thioredoxin. These increased levels of thioredoxin might help stressed B. subtilis cells to maintain the native and reduced state of cellular 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.