Evidence map›Paper›PMID 10850989›Full record

ArticleJournal of bacteriology2000

Role of the dpr product in oxygen tolerance in Streptococcus mutans.

Y Yamamoto, M Higuchi, L B Poole, Y Kamio

Abstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Multiple factors regulate the expression ofFrontiers in cellular and infection microbiology · 2024
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Antibiotic and Antibiofilm Activities ofPathogens (Basel, Switzerland) · 2020
    Article
  12. Article
  13. NADH peroxidase plays a crucial role in consuming HBioscience of microbiota, food and health · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  19. 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

4 authors.

Y YamamotoLaboratory of Applied Microbiology, Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, Amamiya-machi, Aoba-ku, Sendai 981-8555, Japan.
M Higuchi
L B Poole
Y Kamio

Funding

Mechanistic Studies of Alkyl Hydroperoxide Reductase and Related Redox SystemsR01GM050389 · NIGMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 1994 to 2013
$4.8M
NIGMS NIH HHS R01 GM050389
6 · The paper itself

Abstract

We have previously identified and characterized the alkyl hydroperoxide reductase of Streptococcus mutans, which consists of two components, Nox-1 and AhpC. Deletion of both nox-1 and ahpC had no effect on the sensitivity of S. mutans to cumene hydroperoxide or H(2)O(2), implying that the existence of another antioxidant system(s) independent of the Nox-1-AhpC system compensates for the deficiency. Here, a new antioxidant gene (dpr for Dps-like peroxide resistance gene) was isolated from the S. mutans chromosome by its ability to complement an ahpCF deletion mutant of Escherichia coli with a tert-butyl hydroperoxide-hypersensitive phenotype. The dpr gene complemented the defect in peroxidase activity caused by the deletion of nox-1 and ahpC in S. mutans. Under aerobic conditions, the dpr disruption mutant carrying a spectinomycin resistance gene (dpr::Spc(r) mutant) grew as well as wild-type S. mutans in liquid medium. However, the dpr::Spc(r) mutant could not form colonies on an agar plate under air. In addition, neither the dpr::Spc(r) ahpC::Em(r)::nox-1 triple mutant nor the dpr::Spc(r) sod::Em(r) double mutant was able to grow aerobically in liquid medium. The 20-kDa dpr gene product Dpr is an iron-binding protein. Synthesis of Dpr was induced by exposure of S. mutans cells to air. We propose a mechanism by which Dpr confers aerotolerance on S. mutans.

Indexed as

AntioxidantsAerobiosisAmino AcidsBacterial ProteinsBase SequenceCarrier ProteinsCulture MediaDNA, BacterialDNA-Binding ProteinsDrug Resistance, MicrobialFerritinsHydrogen PeroxideIron-Binding ProteinsMolecular Sequence DataMutagenesisOxygenAmino AcidsAntioxidantsBacterial ProteinsCarrier ProteinsCulture MediaDNA, BacterialDNA-Binding ProteinsDPS protein, BacteriaFerritinsHydrogen PeroxideIron-Binding ProteinsOxygenTransferrin-Binding Proteins

Identifiers

PMID10850989
PMCPMC94545

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.