Evidence map›Paper›PMID 21632538›Full record

ArticleThe Journal of biological chemistry2011

Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia.

Beatriz G Guimarães, Rosicler L Barbosa, Adriana S Soprano, Bruna M Campos, Tiago A de Souza, Celisa C C Tonoli, Adriana F P Leme, Mario T Murakami, Celso E Benedetti

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.0field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. In the AlphaproteobacteriumAntioxidants (Basel, Switzerland) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The Sulfide-Responsive SqrR/BigR Homologous Regulator YgaV ofAntioxidants (Basel, Switzerland) · 2022
    Article
  13. The ArsH Protein Product of theAntioxidants (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. HThe Journal of biological chemistry · 2020
    Review
  20. The Response ofmBio · 2020
    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 at 3 institutions in 1 country.

Beatriz G GuimarãesLaboratório Nacional de Biociências, Centro Nacional de Pesquisa em Energia e Materiais, Campinas, São Paulo CP6192, Brazil.
Rosicler L Barbosa
Adriana S Soprano
Bruna M Campos
Tiago A de Souza
Celisa C C Tonoli
Adriana F P Leme
Mario T Murakami
Celso E Benedetti
Brazilian Biosciences National Laboratory · BRBrazilian Center for Research in Energy and Materials · BRLaboratório Nacional de Ciência e Tecnologia do Bioetanol · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Winged-helix transcriptional factors play important roles in the control of gene expression in many organisms. In the plant pathogens Xylella fastidiosa and Agrobacterium tumefaciens, the winged-helix protein BigR, a member of the ArsR/SmtB family of metal sensors, regulates transcription of the bigR operon involved in bacterial biofilm growth. Previous studies showed that BigR represses transcription of its own operon through the occupation of the RNA polymerase-binding site; however, the signals that modulate its activity and the biological function of its operon are still poorly understood. Here we show that although BigR is a homodimer similar to metal sensors, it functions as a novel redox switch that derepresses transcription upon oxidation. Crystal structures of reduced and oxidized BigR reveal that formation of a disulfide bridge involving two critical cysteines induces conformational changes in the dimer that remarkably alter the topography of the winged-helix DNA-binding interface, precluding DNA binding. This structural mechanism of DNA association-dissociation is novel among winged-helix factors. Moreover, we demonstrate that the bigR operon is required for hydrogen sulfide detoxification through the action of a sulfur dioxygenase (Blh) and sulfite exporter. As hydrogen sulfide strongly inhibits cytochrome c oxidase, it must be eliminated to allow aerobic growth under low oxygen tension, an environmental condition found in bacterial biofilms, xylem vessels, and root tissues. Accordingly, we show that the bigR operon is critical to sustain bacterial growth under hypoxia. These results suggest that BigR integrates the transcriptional regulation of a sulfur oxidation pathway to an oxidative signal through a thiol-based redox switch.

Indexed as

Agrobacterium tumefaciensAnimalsBacterial ProteinsBiofilmsConserved SequenceCysteineDioxygenasesDisulfidesDNA, BacterialHydrogen SulfideMiceMitochondrial ProteinsModels, MolecularOperonOxidation-ReductionOxygenBacterial ProteinsCysteineDioxygenasesDisulfidesDNA, BacterialETHE1 protein, mouseHydrogen SulfideMitochondrial ProteinsOxygensulfur dioxygenaseTranscription Factors

Identifiers

PMID21632538
PMCPMC3138302
OpenAlexW1994320541

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.