Evidence map›Paper›PMID 32371489›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Direct observation of helicase-topoisomerase coupling within reverse gyrase.

Xi Yang, Florence Garnier, Hélène Débat, Terence R Strick, Marc Nadal

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. DNA-Topology Simplification by Topoisomerases.Molecules (Basel, Switzerland) · 2021
    Review
  12. DNA topoisomerases: Advances in understanding of cellular roles and multi-protein complexes via structure-function analysis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021
    Review
  13. Archaea: A Gold Mine for Topoisomerase Diversity.Frontiers in microbiology · 2021
    Review
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

5 authors.

Xi YangInstitut de Biologie de l'Ecole Normale Supérieure, 75005 Paris, France.ORCID 0000-0003-0689-1417
Florence GarnierInstitut Jacques Monod, CNRS, UMR7592, Université de Paris, 75205 Paris, France.ORCID 0000-0002-6299-6531
Hélène DébatInstitut Jacques Monod, CNRS, UMR7592, Université de Paris, 75205 Paris, France.ORCID 0000-0003-0020-2748
Terence R StrickInstitut de Biologie de l'Ecole Normale Supérieure, 75005 Paris, France; strick@biologie.ens.fr marc.nadal@ijm.fr.ORCID 0000-0003-1744-3679
Marc NadalInstitut Jacques Monod, CNRS, UMR7592, Université de Paris, 75205 Paris, France; strick@biologie.ens.fr marc.nadal@ijm.fr.ORCID 0000-0001-9637-7694

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reverse gyrases (RGs) are the only topoisomerases capable of generating positive supercoils in DNA. Members of the type IA family, they do so by generating a single-strand break in substrate DNA and then manipulating the two single strands to generate positive topology. Here, we use single-molecule experimentation to reveal the obligatory succession of steps that make up the catalytic cycle of RG. In the initial state, RG binds to DNA and unwinds ∼2 turns of the double helix in an ATP-independent fashion. Upon nucleotide binding, RG then rewinds ∼1 turn of DNA. Nucleotide hydrolysis and/or product release leads to an increase of 2 units of DNA writhe and resetting of the enzyme, for a net change of topology of +1 turn per cycle. Final dissociation of RG from DNA results in rewinding of the 2 turns of DNA that were initially disrupted. These results show how tight coupling of the helicase and topoisomerase activities allows for induction of positive supercoiling despite opposing torque.

Indexed as

Adenosine TriphosphateDNADNA, BacterialDNA-Binding ProteinsDNA HelicasesDNA TopoisomerasesDNA Topoisomerases, Type IModels, MolecularProtein ConformationProtein DomainsThermusAdenosine TriphosphateDNADNA, BacterialDNA-Binding ProteinsDNA HelicasesDNA reverse gyraseDNA TopoisomerasesDNA Topoisomerases, Type IDNA topoisomerasehelicasemagnetic tweezerssingle molecule

Identifiers

PMID32371489
PMCPMC7245102

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.