Evidence map›Paper›PMID 27560944›Full record

ArticlePloS one2016

Regulation of Organic Hydroperoxide Stress Response by Two OhrR Homologs in Pseudomonas aeruginosa.

Sopapan Atichartpongkul, Paiboon Vattanaviboon, Ratiphorn Wisitkamol, Juthamas Jaroensuk, Skorn Mongkolsuk, Mayuree Fuangthong

Abstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Redox protection by bacterial glutathione peroxidase drives virulence inRedox report : communications in free radical research · 2026
    Article
  2. Article
  3. Factors governing the response ofFrontiers in cellular and infection microbiology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Oxidative Stress Response inPathogens (Basel, Switzerland) · 2021
    Review
  9. The MarR-Type Regulator PA3458 Is Involved in Osmoadaptation Control inInternational journal of molecular sciences · 2021
    Article
  10. Regulation ofMicroorganisms · 2021
    Article
  11. Article
  12. Deciphering the Role of Multiple Thioredoxin Fold Proteins ofInternational journal of molecular sciences · 2020
    Article
  13. Article
  14. Article
  15. Article
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

6 authors.

Sopapan AtichartpongkulLaboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand.
Paiboon VattanaviboonLaboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand.
Ratiphorn WisitkamolDepartment of Biotechnology, Faculty of Science, Mahidol University, Bangkok, Thailand.
Juthamas JaroensukApplied Biological Sciences Program, Chulabhorn Graduate Institute, Lak Si, Bangkok, Thailand.
Skorn MongkolsukLaboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand.
Mayuree FuangthongLaboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudomonas aeruginosa ohrR and ospR are gene homologs encoding oxidant sensing transcription regulators. OspR is known to regulate gpx, encoding a glutathione peroxidase, while OhrR regulates the expression of ohr that encodes an organic peroxide specific peroxiredoxin. Here, we show that ospR mediated gpx expression, like ohrR and ohr, specifically responds to organic hydroperoxides as compared to hydrogen peroxide and superoxide anion. Furthermore, the regulation of these two systems is interconnected. OspR is able to functionally complement an ohrR mutant, i.e. it regulates ohr in an oxidant dependent manner. In an ohrR mutant, in which ohr is derepressed, the induction of gpx expression by organic hydroperoxide is reduced. Likewise, in an ospR mutant, where gpx expression is constitutively high, oxidant dependent induction of ohr expression is reduced. Moreover, in vitro binding assays show that OspR binds the ohr promoter, while OhrR binds the gpx promoter, albeit with lower affinity. The binding of OhrR to the gpx promoter may not be physiologically relevant; however, OspR is shown to mediate oxidant-inducible expression at both promoters. Interestingly, the mechanism of OspR-mediated, oxidant-dependent induction at the two promoters appears to be distinct. OspR required two conserved cysteines (C24 and C134) for oxidant-dependent induction of the gpx promoter, while only C24 is essential at the ohr promoter. Overall, this study illustrates possible connection between two regulatory switches in response to oxidative stress.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialGenetic Complementation TestGlutathione PeroxidaseHydrogen PeroxideMutationOxidantsOxidative StressPromoter Regions, GeneticProtein BindingPseudomonas aeruginosaReverse Transcriptase Polymerase Chain ReactionStress, Physiologicaltert-ButylhydroperoxideBacterial ProteinsGlutathione PeroxidaseHydrogen Peroxideorganic hydroperoxide resistance protein, Xanthomonas campestrisOxidantstert-Butylhydroperoxide

Identifiers

PMID27560944
PMCPMC4999210

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.