Evidence map›Paper›PMID 35414142›Full record

ArticleNature communications2022

ComFC mediates transport and handling of single-stranded DNA during natural transformation.

Prashant P Damke, Louisa Celma, Sumedha M Kondekar, Anne Marie Di Guilmi, Stéphanie Marsin, Jordane Dépagne, Xavier Veaute, Pierre Legrand, Hélène Walbott, Julien Vercruyssen and 3 more

Open access · goldAbstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  7. A tripartite protein complex promotes DNA transport during natural transformation in Firmicutes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. ComFB, a widespread family of c-di-NMP receptor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. ComFB, a new widespread family of c-di-NMP receptor proteins.bioRxiv : the preprint server for biology · 2024
    Article
  14. Genetic disruption of the bacterialProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Review
  17. 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

13 authors at 4 institutions in 1 country.

Prashant P Damke *Université Paris-Saclay, CEA, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France.ORCID http://orcid.org/0000-0001-5109-1756
Louisa Celma *Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0002-6473-8915
Sumedha M KondekarUniversité Paris-Saclay, CEA, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France.ORCID http://orcid.org/0000-0003-1416-5466
Anne Marie Di GuilmiUniversité Paris-Saclay, CEA, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France.
Stéphanie MarsinUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0002-7074-7818
Jordane DépagneUniversité Paris-Saclay, CEA, INSERM, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France.
Xavier VeauteUniversité Paris-Saclay, CEA, INSERM, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France.ORCID http://orcid.org/0000-0003-4868-247X
Pierre LegrandSynchrotron SOLEIL, L'Orme des Merisiers, F-91192, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0003-2431-2255
Hélène WalbottUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0002-0438-9493
Julien VercruyssenUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France.
Raphaël GuéroisUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0001-5294-2858
Sophie Quevillon-CheruelUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), F-91198, Gif-sur-Yvette, France. sophie.quevillon-cheruel@i2bc.paris-saclay.fr.
J Pablo RadicellaUniversité Paris-Saclay, CEA, Stabilité Génétique Cellules Souches et Radiations, Institut de Biologie François Jacob, F-92260, Fontenay aux Roses, France. pablo.radicella@cea.fr.ORCID http://orcid.org/0000-0002-8807-7226
Centre National de la Recherche Scientifique · FRUniversité Paris Cité · FRInserm · FRSynchrotron soleil · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ComFC protein is essential for natural transformation, a process that plays a major role in the spread of antibiotic resistance genes and virulence factors across bacteria. However, its role remains largely unknown. Here, we show that Helicobacter pylori ComFC is involved in DNA transport through the cell membrane, and is required for the handling of the single-stranded DNA once it is delivered into the cytoplasm. The crystal structure of ComFC includes a zinc-finger motif and a putative phosphoribosyl transferase domain, both necessary for the protein's in vivo activity. Furthermore, we show that ComFC is a membrane-associated protein with affinity for single-stranded DNA. Our results suggest that ComFC provides the link between the transport of the transforming DNA into the cytoplasm and its handling by the recombination machinery.

Indexed as

DNA, Single-StrandedHelicobacter pyloriBacterial ProteinsDNAMembrane ProteinsTransformation, BacterialBacterial ProteinsDNADNA, Single-StrandedMembrane Proteins

Identifiers

PMID35414142
PMCPMC9005727
OpenAlexW4223537406

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.