Evidence map›Paper›PMID 25398878›Full record

ArticleThe Journal of biological chemistry2014

Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation.

Jong Gyu Lim, Ye-Ji Bang, Sang Ho Choi

Open access · hybridAbstract read
In one paragraph

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Fe-S cluster homeostasis and beyond: The multifaceted roles of IscR.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Screening of Anti-Adhesion Agents for PathogenicJournal of microbiology and biotechnology · 2023
    Article
  9. Article
  10. Article
  11. Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. A Regulatory Network ControlsFrontiers in microbiology · 2019
    Article
  17. Article
  18. Identification and characterization ofThe Journal of biological chemistry · 2017
    Article
  19. The hydrogen peroxide hypersensitivity of OxyR2 inThe Journal of biological chemistry · 2017
    Article
  20. 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

3 authors at 1 institution in 1 country.

Jong Gyu LimFrom the National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Seoul National University, Seoul 151-921, South Korea.
Ye-Ji BangFrom the National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Seoul National University, Seoul 151-921, South Korea.
Sang Ho ChoiFrom the National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Seoul National University, Seoul 151-921, South Korea choish@snu.ac.kr.
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxiredoxins (Prxs) are ubiquitous antioxidant enzymes that reduce toxic peroxides. A new Vibrio vulnificus Prx, named Prx3, was identified and characterized in this study. Biochemical and mutational analyses revealed that Prx3 reduces H2O2, utilizing glutaredoxin 3 (Grx3) and glutathione (GSH) as reductants, and requires only N-terminal peroxidatic cysteine for its catalysis. These results, combined with the monomeric size of Prx3 observed under non-reducing conditions, suggested that Prx3 is a Grx3/GSH-dependent 1-Cys Prx and oxidized without forming intermolecular disulfide bonds. The prx3 mutation impaired growth in the medium containing peroxides and reduced virulence in mice, indicating that Prx3 is essential for survival under oxidative stress and pathogenesis of V. vulnificus. The Fe-S cluster regulator IscR activates prx3 by direct binding to a specific binding sequence centered at -44 from the transcription start site. The binding sequence was homologous to the Type 2 IscR-binding sequence, most likely recognized by the Fe-S clusterless apo-IscR in Escherichia coli. The iscR3CA mutant, chromosomally encoding the apo-locked IscR, exhibited 3-fold higher levels of activation of prx3 than the wild type and accumulated more IscR3CA protein in cells. The IscR-dependent activation of prx3 by aerobic growth and iron starvation was also associated with the increase in cellular levels of IscR protein. Taken together, the results suggested that IscR senses iron starvation as well as reactive oxygen species and shifts to the apo-form, which leads to the increase of cellular IscR and in turn prx3 expression, contributing to the survival and virulence of V. vulnificus during pathogenesis.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsBase SequenceBinding SitesFemaleGene Expression Regulation, BacterialIronMice, Inbred ICRMicrobial ViabilityMolecular Sequence DataOxidative StressPeroxiredoxin IIIPromoter Regions, GeneticTranscription, GeneticVibrio InfectionsBacterial ProteinsIronPeroxiredoxin IIIBacterial PathogenesisGene RegulationIron StarvationIscROxidative StressPeroxiredoxinReactive Oxygen Species (ROS)Vibrio vulnificus

Identifiers

PMID25398878
PMCPMC4276887
OpenAlexW2020165779

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.