Evidence map›Paper›PMID 12081946›Full record

ArticleJournal of bacteriology2002

A Salmonella enterica serovar typhimurium hemA mutant is highly susceptible to oxidative DNA damage.

Maya Elgrably-Weiss, Sunny Park, Eliana Schlosser-Silverman, Ilan Rosenshine, James Imlay, Shoshy Altuvia

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.5field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Stress Response Mechanisms ofFoods (Basel, Switzerland) · 2022
    Article
  3. Review
  4. Genome-wide survey of codons under diversifying selection in a highly recombining bacterial species, Helicobacter pylori.DNA research : an international journal for rapid publication of reports on genes and genomes · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other Alpha-proteobacteria.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 at 2 institutions in 2 countries.

Maya Elgrably-WeissDepartment of Molecular Genetics and Biotechnology, The Hebrew University-Hadassah Medical School, 91120 Jerusalem, Israel.
Sunny Park
Eliana Schlosser-Silverman
Ilan Rosenshine
James Imlay
Shoshy Altuvia
Hebrew University of Jerusalem · ILUniversity of Illinois Urbana-Champaign · US

Funding

MECHANISM OF OXIDATIVE DNA DAMAGE IN MODEL ORGANISMSR01GM059030 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 1999 to 2002
$306k
NIGMS NIH HHS GM59030
6 · The paper itself

Abstract

The first committed step in the biosynthesis of heme, an important cofactor of two catalases and a number of cytochromes, is catalyzed by the hemA gene product. Salmonella enterica serovar Typhimurium hemA26::Tn10d (hemA26) was identified in a genetic screen of insertion mutants that were sensitive to hydrogen peroxide. Here we show that the hemA26 mutant respires at half the rate of wild-type cells and is highly susceptible to the effects of oxygen species. Exposure of the hemA26 strain to hydrogen peroxide results in extensive DNA damage and cell death. The chelation of intracellular free iron fully abrogates the sensitivity of this mutant, indicating that the DNA damage results from the iron-catalyzed formation of hydroxyl radicals. The inactivation of heme synthesis does not change the amount of intracellular iron, but by diminishing the rate of respiration, it apparently increases the amount of reducing equivalents available to drive the Fenton reaction. We also report that hydrogen peroxide has opposite effects on the expression of hemA and hemH, the first and last genes of heme biosynthesis pathway, respectively. hemA mRNA levels decrease, while the transcription of hemH is induced by hydrogen peroxide, in an oxyR-dependent manner. The oxyR-dependent induction is suppressed under conditions that accelerate the Fenton reaction by a mechanism that is not yet understood.

Indexed as

DNA-Binding ProteinsDNA DamageAldehyde OxidoreductasesBase SequenceGene Expression Regulation, BacterialHydrogen PeroxideIronMolecular Sequence DataMutationOxidation-ReductionRepressor ProteinsSalmonella typhimuriumTranscription FactorsAldehyde OxidoreductasesDNA-Binding Proteinsglutamyl tRNA reductaseHydrogen PeroxideIronRepressor ProteinsTranscription Factors

Identifiers

PMID12081946
PMCPMC135181
OpenAlexW2053994975

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.