Evidence map›Paper›PMID 22238377›Full record

ArticleNucleic acids research2012

Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.

Gottfried J Palm, Bui Khanh Chi, Paul Waack, Katrin Gronau, Dörte Becher, Dirk Albrecht, Winfried Hinrichs, Randy J Read, Haike Antelmann

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The ArsH Protein Product of theAntioxidants (Basel, Switzerland) · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Disulfide Stress Response and ProteinAntioxidants (Basel, Switzerland) · 2019
    Article
  12. An EmrB multidrug efflux pump inThe Journal of biological chemistry · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Two distinct mechanisms of transcriptional regulation by the redox sensor YodB.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

9 authors.

Gottfried J PalmInstitute for Biochemistry, Ernst-Moritz-Arndt-University of Greifswald, D-17487 Greifswald, Germany.
Bui Khanh Chi
Paul Waack
Katrin Gronau
Dörte Becher
Dirk Albrecht
Winfried Hinrichs
Randy J Read
Haike Antelmann

Funding

Wellcome Trust 082961
6 · The paper itself

Abstract

Bacillus subtilis encodes redox-sensing MarR-type regulators of the OhrR and DUF24-families that sense organic hydroperoxides, diamide, quinones or aldehydes via thiol-based redox-switches. In this article, we characterize the novel redox-sensing MarR/DUF24-family regulator HypR (YybR) that is activated by disulphide stress caused by diamide and NaOCl in B. subtilis. HypR controls positively a flavin oxidoreductase HypO that confers protection against NaOCl stress. The conserved N-terminal Cys14 residue of HypR has a lower pK(a) of 6.36 and is essential for activation of hypO transcription by disulphide stress. HypR resembles a 2-Cys-type regulator that is activated by Cys14-Cys49' intersubunit disulphide formation. The crystal structures of reduced and oxidized HypR proteins were resolved revealing structural changes of HypR upon oxidation. In reduced HypR a hydrogen-bonding network stabilizes the reactive Cys14 thiolate that is 8-9 Å apart from Cys49'. HypR oxidation breaks these H-bonds, reorients the monomers and moves the major groove recognition α4 and α4' helices ∼4 Å towards each other. This is the first crystal structure of a redox-sensing MarR/DUF24 family protein in bacteria that is activated by NaOCl stress. Since hypochloric acid is released by activated macrophages, related HypR-like regulators could function to protect pathogens against the host immune defense.

Indexed as

Gene Expression Regulation, BacterialTranscriptional ActivationBacillus subtilisBacterial ProteinsBase SequenceCysteineDiamideDNA-Binding ProteinsModels, MolecularMolecular Sequence DataNitroreductasesOperator Regions, GeneticOxidation-ReductionOxidoreductasesSodium HypochloriteStress, PhysiologicalBacterial ProteinsCysteineDiamideDNA-Binding ProteinsNitroreductasesOxidoreductasesSodium HypochloriteTrans-Activators

Identifiers

PMID22238377
PMCPMC3351151

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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.