Evidence map›Paper›PMID 30814507›Full record

ArticleNature communications2019

A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT.

Ariel Talavera, Hedvig Tamman, Andres Ainelo, Albert Konijnenberg, San Hadži, Frank Sobott, Abel Garcia-Pino, Rita Hõrak, Remy Loris

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Biochemical and X-ray analyses of the players involved in the faRel2/aTfaRel2 toxin-antitoxin operon.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.Acta crystallographica. Section D, Structural biology · 2021
    Article
  11. Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021
    Review
  12. Article
  13. The DisorderedMicroorganisms · 2021
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Toxins · 2019
    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 at 4 institutions in 4 countries.

Ariel TalaveraStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, B-1050, Brussel, Belgium. atalaver@ulb.ac.be.
Hedvig TammanInstitute of Molecular and Cell Biology, University of Tartu, 51010, Tartu, Estonia.
Andres AineloInstitute of Molecular and Cell Biology, University of Tartu, 51010, Tartu, Estonia.
Albert KonijnenbergStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, B-1050, Brussel, Belgium.
San HadžiStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, B-1050, Brussel, Belgium.
Frank SobottBiomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Groenenborgerlaan 171, B-2020, Antwerpen, Belgium.
Abel Garcia-PinoBiologie Structurale et Biophysique, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, B-6041, Gosselies, Belgium.ORCID http://orcid.org/0000-0002-0634-0300
Rita HõrakInstitute of Molecular and Cell Biology, University of Tartu, 51010, Tartu, Estonia.
Remy LorisStructural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, B-1050, Brussel, Belgium. remy.loris@vub.be.
Vrije Universiteit Brussel · BEUniversity of Tartu · EEUniversité Libre de Bruxelles · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraT

Indexed as

AntitoxinsBacterial ProteinsBacterial ToxinsDNA, BacterialGenes, BacterialIntrinsically Disordered ProteinsModels, MolecularNucleic Acid ConformationOperonPromoter Regions, GeneticProtein BindingProtein FoldingProtein Structure, QuaternaryPseudomonas putidaStatic ElectricityToxin-Antitoxin SystemsAntitoxinsBacterial ProteinsBacterial ToxinsDNA, BacterialIntrinsically Disordered Proteins

Identifiers

PMID30814507
PMCPMC6393540
OpenAlexW2915535827

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.