Evidence map›Paper›PMID 26663076›Full record

ArticleThe Journal of biological chemistry2016

DNA Gyrase Is the Target for the Quinolone Drug Ciprofloxacin in Arabidopsis thaliana.

Katherine M Evans-Roberts, Lesley A Mitchenall, Melisa K Wall, Julie Leroux, Joshua S Mylne, Anthony Maxwell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Antibacterial Activity, Phytochemical AnalysisIndian journal of microbiology · 2025
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  4. Review
  5. Article
  6. Review
  7. Royal Society open science · 2023
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B.Antimicrobial agents and chemotherapy · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  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

6 authors at 4 institutions in 2 countries.

Katherine M Evans-RobertsFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Lesley A MitchenallFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Melisa K WallFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Julie Lerouxthe School of Chemistry and Biochemistry, University of Western Australia, 35 Stirling Highway, Crawley, Perth 6009, Australia, and the Australian Research Council Centre of Excellence in Plant Energy Biology, 35 Stirling Highway, Crawley, Perth 6009, Australia.
Joshua S Mylnethe School of Chemistry and Biochemistry, University of Western Australia, 35 Stirling Highway, Crawley, Perth 6009, Australia, and the Australian Research Council Centre of Excellence in Plant Energy Biology, 35 Stirling Highway, Crawley, Perth 6009, Australia.
Anthony MaxwellFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom, tony.maxwell@jic.ac.uk.
John Innes Centre · GBNorwich Research Park · GBARC Centre of Excellence in Plant Energy Biology · AUUniversity of Western Australia · AU

Funding

Biotechnology and Biological Sciences Research Council BB/J004561/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000201
6 · The paper itself

Abstract

The Arabidopsis thaliana genome contains four genes that were originally annotated as potentially encoding DNA gyrase: ATGYRA, ATGYRB1, ATGYRB2, and ATGYRB3. Although we subsequently showed that ATGYRB3 does not encode a gyrase subunit, the other three genes potentially encode subunits of a plant gyrase. We also showed evidence for the existence of supercoiling activity in A. thaliana and that the plant is sensitive to quinolone and aminocoumarin antibiotics, compounds that target DNA gyrase in bacteria. However, it was not possible at that time to show whether the A. thaliana genes encoded an active gyrase enzyme, nor whether that enzyme is indeed the target for the quinolone and aminocoumarin antibiotics. Here we show that an A. thaliana mutant resistant to the quinolone drug ciprofloxacin has a point mutation in ATGYRA. Moreover we show that, as in bacteria, the quinolone-sensitive (wild-type) allele is dominant to the resistant gene. Further we have heterologously expressed ATGYRA and ATGYRB2 in a baculovirus expression system and shown supercoiling activity of the partially purified enzyme. Expression/purification of the quinolone-resistant A. thaliana gyrase yields active enzyme that is resistant to ciprofloxacin. Taken together these experiments now show unequivocally that A. thaliana encodes an organelle-targeted DNA gyrase that is the target of the quinolone drug ciprofloxacin; this has important consequences for plant physiology and the development of herbicides.

Indexed as

Amino Acid SubstitutionAnimalsAnti-Bacterial AgentsArabidopsisArabidopsis ProteinsChloroplastsCiprofloxacinDNA GyraseDrug ResistanceGene Knockout TechniquesMitochondriaOrganelle ShapePlant LeavesPlants, Genetically ModifiedPoint MutationProtein ConformationAnti-Bacterial AgentsArabidopsis ProteinsCiprofloxacinDNA GyraseProtein SubunitsRecombinant ProteinsTopoisomerase II InhibitorschloroplastDNA gyraseDNA replicationDNA topoisomeraseplant biochemistryquinolones

Identifiers

PMID26663076
PMCPMC4751362
OpenAlexW2192174486

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.