Evidence map›Paper›PMID 22936808›Full record

ArticleThe Journal of biological chemistry2012

Structural basis for intrinsic thermosensing by the master virulence regulator RovA of Yersinia.

Nick Quade, Chriselle Mendonca, Katharina Herbst, Ann Kathrin Heroven, Christiane Ritter, Dirk W Heinz, Petra Dersch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
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  4. The cycle of infectious fever - how it affects bacterial infections.Frontiers in cellular and infection microbiology · 2026
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  6. Article
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  9. An EmrB multidrug efflux pump inThe Journal of biological chemistry · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. AllFrontiers in cellular and infection microbiology · 2018
    Review
  15. Article
  16. Review
  17. Review
  18. Environmental Regulation of Yersinia Pathophysiology.Frontiers in cellular and infection microbiology · 2016
    Review
  19. Review
  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 2 institutions in 2 countries.

Nick QuadeDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
Chriselle Mendonca
Katharina Herbst
Ann Kathrin Heroven
Christiane Ritter
Dirk W Heinz
Petra Dersch
Helmholtz Centre for Infection Research · DEInstitute of Structural and Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathogens often rely on thermosensing to adjust virulence gene expression. In yersiniae, important virulence-associated traits are under the control of the master regulator RovA, which uses a built-in thermosensor to control its activity. Thermal upshifts encountered upon host entry induce conformational changes in the RovA dimer that attenuate DNA binding and render the protein more susceptible to proteolysis. Here, we report the crystal structure of RovA in the free and DNA-bound forms and provide evidence that thermo-induced loss of RovA activity is promoted mainly by a thermosensing loop in the dimerization domain and residues in the adjacent C-terminal helix. These determinants allow partial unfolding of the regulator upon an upshift to 37 °C. This structural distortion is transmitted to the flexible DNA-binding domain of RovA. RovA contacts mainly the DNA backbone in a low-affinity binding mode, which allows the immediate release of RovA from its operator sites. We also show that SlyA, a close homolog of RovA from Salmonella with a very similar structure, is not a thermosensor and remains active and stable at 37 °C. Strikingly, changes in only three amino acids, reflecting evolutionary replacements in SlyA, result in a complete loss of the thermosensing properties of RovA and prevent degradation. In conclusion, only minor alterations can transform a thermotolerant regulator into a thermosensor that allows adjustment of virulence and fitness determinants to their thermal environment.

Indexed as

Protein FoldingBacterial ProteinsDNA, BacterialHot TemperatureProtein BindingProtein Structure, TertiaryProteolysisSalmonellaStructural Homology, ProteinStructure-Activity RelationshipTranscription FactorsVirulence FactorsYersinia pseudotuberculosisBacterial ProteinsDNA, BacterialRovA protein, YersiniaTranscription FactorsVirulence Factors

Identifiers

PMID22936808
PMCPMC3476249
OpenAlexW2025430318

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.