Evidence map›Paper›PMID 40425557›Full record

ArticleNature communications2025

Cryo-EM Structure of the relaxosome, a complex essential for bacterial mating and the spread of antibiotic resistance genes.

Sunanda M Williams, Sandra Raffl, Sabine Kienesberger, Aravindan Ilangovan, Ellen L Zechner, Gabriel Waksman

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. 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

6 authors.

Sunanda M WilliamsInstitute of Structural and Molecular Biology, School of Natural Sciences, Birkbeck College, Malet Street, London, WC1E 7HX, UK. sunanda.williams@bbk.ac.uk.ORCID http://orcid.org/0000-0003-0558-5565
Sandra RafflInstitute of Molecular Biosciences, University of Graz, BioTechMed-Graz, Humboldtstrasse 50, 8010, Graz, Austria.
Sabine KienesbergerInstitute of Molecular Biosciences, University of Graz, BioTechMed-Graz, Humboldtstrasse 50, 8010, Graz, Austria.ORCID http://orcid.org/0000-0003-3190-3678
Aravindan IlangovanInstitute of Structural and Molecular Biology, School of Natural Sciences, Birkbeck College, Malet Street, London, WC1E 7HX, UK.ORCID http://orcid.org/0000-0002-0391-3812
Ellen L ZechnerInstitute of Molecular Biosciences, University of Graz, BioTechMed-Graz, Humboldtstrasse 50, 8010, Graz, Austria.ORCID http://orcid.org/0000-0003-2035-1898
Gabriel WaksmanInstitute of Structural and Molecular Biology, School of Natural Sciences, Birkbeck College, Malet Street, London, WC1E 7HX, UK. g.waksman@bbk.ac.uk.ORCID http://orcid.org/0000-0003-0708-2726

Funding

Wellcome TrustWellcome Trust (Wellcome) 217089/Z/19/Z
6 · The paper itself

Abstract

Bacterial mating, or conjugation, was discovered nearly 80 years ago as a process transferring genes from one bacterial cell (the donor) to another (the recipient). It requires three key multiprotein complexes in the donor cell: a DNA-processing machinery called the relaxosome, a double-membrane spanning type 4 secretion system (T4SS), and an extracellular appendage termed pilus. While the near-atomic resolution structures of the T4SS and pilus are already known, that of the relaxosome has not been reported to date. Here, we describe the cryo-EM structure of the fully assembled relaxosome encoded by the paradigm F plasmid in two different states corresponding to distinct functional steps along the DNA processing reaction. By varying the structures of model DNAs we delineate conformational changes required to initiate conjugation. Mutational studies of the various protein-protein and protein-DNA interaction hubs suggest a complex sensitive to trigger signals, that could arise from cell-to-cell contacts with recipient cells.

Indexed as

Conjugation, GeneticEscherichia coliType IV Secretion SystemsBacterial ProteinsCryoelectron MicroscopyDNA, BacterialF FactorFimbriae, BacterialModels, MolecularBacterial ProteinsDNA, BacterialType IV Secretion Systems

Identifiers

PMID40425557
PMCPMC12117103

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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.