Evidence map›Paper›PMID 35246533›Full record

ArticleNature communications2022

The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation.

Sebastian A G Braus, Francesca L Short, Stefanie Holz, Matthew J M Stedman, Alvar D Gossert, Manuela K Hospenthal

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  12. DNA binding is rate-limiting for natural transformation.bioRxiv : the preprint server for biology · 2024
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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 2 institutions in 2 countries.

Sebastian A G BrausInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-1263-2107
Francesca L ShortDepartment of Microbiology, Monash University, 19 Innovation Walk, Clayton, 3800, Victoria, Australia.ORCID http://orcid.org/0000-0002-0025-4858
Stefanie Holz *Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, Switzerland.
Matthew J M Stedman *Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, Switzerland.
Alvar D GossertInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-7732-495X
Manuela K HospenthalInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, Switzerland. manuela.hospenthal@mol.biol.ethz.ch.ORCID http://orcid.org/0000-0003-1175-6826
ETH Zurich · CHMonash University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Naturally competent bacteria encode sophisticated protein machinery for the uptake and translocation of exogenous DNA into the cell. If this DNA is integrated into the bacterial genome, the bacterium is said to be naturally transformed. Most competent bacterial species utilise type IV pili for the initial DNA uptake step. These proteinaceous cell-surface structures are composed of thousands of pilus subunits (pilins), designated as major or minor according to their relative abundance in the pilus. Here, we show that the minor pilin FimT plays an important role in the natural transformation of Legionella pneumophila. We use NMR spectroscopy, in vitro DNA binding assays and in vivo transformation assays to understand the molecular basis of FimT's role in this process. FimT binds to DNA via an electropositive patch, rich in arginines, several of which are well-conserved and located in a conformationally flexible C-terminal tail. FimT orthologues from other Gammaproteobacteria share the ability to bind to DNA. Our results suggest that FimT plays an important role in DNA uptake in a wide range of competent species.

Indexed as

Fimbriae ProteinsLegionella pneumophilaBacterial ProteinsDNADNA, BacterialFimbriae, BacterialTransformation, BacterialBacterial ProteinsDNADNA, BacterialFimbriae Proteins

Identifiers

PMID35246533
PMCPMC8897410
OpenAlexW4220900123

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.