Evidence map›Paper›PMID 36257990›Full record

ArticleNature communications2022

Structural insight into Tn3 family transposition mechanism.

Alexander V Shkumatov, Nicolas Aryanpour, Cédric A Oger, Gérôme Goossens, Bernard F Hallet, Rouslan G Efremov

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Soil management practices shape the abundance, diversity, and spread of antimicrobial resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Genome Evolution in Plant Pathogenic Bacteria.Genome biology and evolution · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Mobile genetic elements inJournal of bacteriology · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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.

Alexander V ShkumatovCenter for Structural Biology, Vlaams Instituut voor Biotechnologie, Brussels, Belgium.ORCID 0000-0001-7281-9291
Nicolas AryanpourLouvain Institue of Biomolecular Science and Technology, Université Catholique de Louvain (UCLouvain), Croix du Sud 4/5, 1348, Louvain-la-Neuve, Belgium.ORCID 0000-0001-9635-3465
Cédric A OgerLouvain Institue of Biomolecular Science and Technology, Université Catholique de Louvain (UCLouvain), Croix du Sud 4/5, 1348, Louvain-la-Neuve, Belgium.ORCID 0000-0002-7604-0653
Gérôme GoossensLouvain Institue of Biomolecular Science and Technology, Université Catholique de Louvain (UCLouvain), Croix du Sud 4/5, 1348, Louvain-la-Neuve, Belgium.
Bernard F HalletLouvain Institue of Biomolecular Science and Technology, Université Catholique de Louvain (UCLouvain), Croix du Sud 4/5, 1348, Louvain-la-Neuve, Belgium. bernard.hallet@uclouvain.be.ORCID 0000-0001-6707-6382
Rouslan G EfremovCenter for Structural Biology, Vlaams Instituut voor Biotechnologie, Brussels, Belgium. rouslan.efremov@vub.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transposons are diverse mobile genetic elements that play the critical role as genome architects in all domains of life. Tn3 is a widespread family and among the first identified bacterial transposons famed for their contribution to the dissemination of antibiotic resistance. Transposition within this family is mediated by a large TnpA transposase, which facilitates both transposition and target immunity. Howtever, a structural framework required for understanding the mechanism of TnpA transposition is lacking. Here, we describe the cryo-EM structures of TnpA from Tn4430 in the apo form and paired with transposon ends before and after DNA cleavage and strand transfer. We show that TnpA has an unusual architecture and exhibits a family specific regulatory mechanism involving metamorphic refolding of the RNase H-like catalytic domain. The TnpA structure, constrained by a double dimerization interface, creates a peculiar topology that suggests a specific role for the target DNA in transpososome assembly and activation.

Indexed as

DNA Transposable ElementsEscherichia coliRibonuclease HTransposasesDNA Transposable ElementsRibonuclease HTransposases

Identifiers

PMID36257990
PMCPMC9579193

What OpenQuestion holds

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Registered trials

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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.