Evidence map›Paper›PMID 22609922›Full record

ArticleJournal of bacteriology2012

Pseudomonas aeruginosa thiol peroxidase protects against hydrogen peroxide toxicity and displays atypical patterns of gene regulation.

Nawarat Somprasong, Thichakorn Jittawuttipoka, Jintana Duang-Nkern, Adisak Romsang, Pimchai Chaiyen, Herbert P Schweizer, Paiboon Vattanaviboon, Skorn Mongkolsuk

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. The roles of theJournal of bacteriology · 2026
    Article
  2. Asphaltene biotransformation by a novel enzyme thiol peroxidase fromApplied and environmental microbiology · 2025
    Article
  3. Review
  4. Global transcriptional response of Pseudomonas aeruginosa to UVA radiation.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article
  5. Identification of the organic peroxide scavenging system ofApplied and environmental microbiology · 2024
    Article
  6. Fe-S cluster homeostasis and beyond: The multifaceted roles of IscR.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  7. Eco-evolutionary dynamics of experimentalMicrobiology (Reading, England) · 2023
    Article
  8. Detoxification Response ofMicroorganisms · 2022
    Article
  9. Article
  10. Article
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  15. Article
  16. Article
  17. Pseudomonas aeruginosamSphere · 2018
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Nawarat SomprasongLaboratory of Biotechnology, Chulabhorn Research Institute Lak Si, Bangkok, Thailand.
Thichakorn Jittawuttipoka
Jintana Duang-Nkern
Adisak Romsang
Pimchai Chaiyen
Herbert P Schweizer
Paiboon Vattanaviboon
Skorn Mongkolsuk
Chulabhorn Research Institute · THMahidol University · THColorado State University · USMinistry of Education · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Pseudomonas aeruginosa PAO1 thiol peroxidase homolog (Tpx) belongs to a family of enzymes implicated in the removal of toxic peroxides. We have shown the expression of tpx to be highly inducible with redox cycling/superoxide generators and diamide and weakly inducible with organic hydroperoxides and hydrogen peroxide (H(2)O(2)). The PAO1 tpx pattern is unlike the patterns for other peroxide-scavenging genes in P. aeruginosa. Analysis of the tpx promoter reveals the presence of a putative IscR binding site located near the promoter. The tpx expression profiles in PAO1 and the iscR mutant, together with results from gel mobility shift assays showing that purified IscR specifically binds the tpx promoter, support the role of IscR as a transcriptional repressor of tpx that also regulates the oxidant-inducible expression of the gene. Recombinant Tpx has been purified and biochemically characterized. The enzyme catalyzes thioredoxin-dependent peroxidation and can utilize organic hydroperoxides and H(2)O(2) as substrates. The Δtpx mutant demonstrates differential sensitivity to H(2)O(2) only at moderate concentrations (0.5 mM) and not at high (20 mM) concentrations, suggesting a novel protective role of tpx against H(2)O(2) in P. aeruginosa. Altogether, P. aeruginosa tpx is a novel member of the IscR regulon and plays a primary role in protecting the bacteria from submillimolar concentrations of H(2)O(2).

Indexed as

Gene Expression Regulation, BacterialBinding SitesDNA, BacterialElectrophoretic Mobility Shift AssayGene DeletionGene Expression ProfilingHydrogen PeroxidePeroxidasePromoter Regions, GeneticProtein BindingPseudomonas aeruginosaRegulonRepressor ProteinsSulfhydryl CompoundsDNA, BacterialHydrogen PeroxidePeroxidaseRepressor ProteinsSulfhydryl Compounds

Identifiers

PMID22609922
PMCPMC3416540
OpenAlexW2140709203

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.