Evidence map›Paper›PMID 18487332›Full record

ArticleJournal of bacteriology2008

Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus.

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, Michael Hecker

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DecipheringmSystems · 2024
    Article
  5. Article
  6. Ecophysiological Study ofApplied and environmental microbiology · 2020
    Article
  7. Article
  8. Article
  9. TheFrontiers in microbiology · 2017
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Review
  17. Article
  18. Bacillithiol: a key protective thiol in Staphylococcus aureus.Expert review of anti-infective therapy · 2015
    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

7 authors at 1 institution in 1 country.

Falko HochgräfeInstitut für Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald, Greifswald, Germany.
Carmen Wolf
Stephan Fuchs
Manuel Liebeke
Michael Lalk
Susanne Engelmann
Michael Hecker
Universität Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nonpathogenic Bacillus subtilis and the pathogen Staphylococcus aureus are gram-positive model organisms that have to cope with the radical nitric oxide (NO) generated by nitrite reductases of denitrifying bacteria and by the inducible NO synthases of immune cells of the host, respectively. The response of both microorganisms to NO was analyzed by using a two-dimensional gel approach. Metabolic labeling of the proteins revealed major changes in the synthesis pattern of cytosolic proteins after the addition of the NO donor MAHMA NONOate. Whereas B. subtilis induced several oxidative stress-responsive regulons controlled by Fur, PerR, OhrR, and Spx, as well as the general stress response controlled by the alternative sigma factor SigB, the more resistant S. aureus showed an increased synthesis rate of proteins involved in anaerobic metabolism. These data were confirmed by nuclear magnetic resonance analyses indicating that NO causes a drastically higher increase in the formation of lactate and butanediol in S. aureus than in B. subtilis. Monitoring the intracellular protein thiol state, we observed no increase in reversible or irreversible protein thiol modifications after NO stress in either organism. Obviously, NO itself does not cause general protein thiol oxidations. In contrast, exposure of cells to NO prior to peroxide stress diminished the irreversible thiol oxidation caused by hydrogen peroxide.

Indexed as

Anti-Bacterial AgentsBacillus subtilisBacterial ProteinsButylene GlycolsElectrophoresis, Gel, Two-DimensionalGene Expression Regulation, BacterialLactic AcidMagnetic Resonance SpectroscopyNitric OxideProteomeStaphylococcus aureusSulfhydryl CompoundsAnti-Bacterial AgentsBacterial ProteinsButylene GlycolsLactic AcidNitric OxideProteomeSulfhydryl Compounds

Identifiers

PMID18487332
PMCPMC2447014
OpenAlexW2162404434

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.