Evidence map›Paper›PMID 35041498›Full record

ArticleJournal of bacteriology2022

Natural Transformation Protein ComFA Exhibits Single-Stranded DNA Translocase Activity.

Hannah R Foster, Xiaoxuan Lin, Sriram Srikant, Rachel R Cueny, Tanya G Falbel, James L Keck, Rachelle Gaudet, Briana M Burton

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-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

8 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. 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
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. 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

8 authors at 2 institutions in 1 country.

Hannah R FosterDepartment of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID 0000-0003-4683-6180
Xiaoxuan LinDepartment of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Sriram SrikantDepartment of Molecular and Cellular Biology, Harvard Universitygrid.38142.3c, Cambridge, Massachusetts, USA.
Rachel R CuenyDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Tanya G FalbelDepartment of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA.
James L KeckDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID 0000-0002-5961-0220
Rachelle GaudetDepartment of Molecular and Cellular Biology, Harvard Universitygrid.38142.3c, Cambridge, Massachusetts, USA.
Briana M BurtonDepartment of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID 0000-0002-6444-8213
University of Wisconsin–Madison · USHarvard University · US

Funding

Mechanism of Divalent Metal Transport by NRamp-Family TransportersR01GM120996 · NIGMS · HARVARD UNIVERSITY · PI GAUDET, RACHELLE · 2017 to 2024
$3.0M
Membrane-associated DNA transport machines in Bacillus subtilisR01GM121865 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURTON, BRIANA M. · 2017 to 2021
$1.9M
Howard Hughes Medical Institute International Research ScholarNIGMS NIH HHS R01 GM120996NIGMS NIH HHS R01 GM121865NIH HHS R01-GM120996NIH HHS R01-GM121865
6 · The paper itself

Abstract

Natural transformation is one of the major mechanisms of horizontal gene transfer in bacterial populations and has been demonstrated in numerous species of bacteria. Despite the prevalence of natural transformation, much of the molecular mechanism remains unexplored. One major outstanding question is how the cell powers DNA import, which is rapid and highly processive. ComFA is one of a few proteins required for natural transformation in Gram-positive bacteria. Its structural resemblance to the DEAD box helicase family has led to a long-held hypothesis that ComFA acts as a motor to help drive DNA import into the cytosol. Here, we explored the helicase and translocase activity of ComFA to address this hypothesis. We followed the DNA-dependent ATPase activity of ComFA and, combined with mathematical modeling, demonstrated that ComFA likely translocates on single-stranded DNA from 5' to 3'. However, this translocase activity does not lead to DNA unwinding under the conditions we tested. Further, we analyzed the ATPase cycle of ComFA and found that ATP hydrolysis stimulates the release of DNA, providing a potential mechanism for translocation. These findings help define the molecular contribution of ComFA to natural transformation and support the conclusion that ComFA plays a key role in powering DNA uptake.

Indexed as

Adenosine TriphosphatasesDNA, Single-StrandedAdenosine TriphosphateDEAD-box RNA HelicasesDNADNA HelicasesAdenosine TriphosphatasesAdenosine TriphosphateDEAD-box RNA HelicasesDNADNA HelicasesDNA, Single-StrandedATPasecompetenceDExD-boxDNA helicasehelicasenatural transformation

Identifiers

PMID35041498
PMCPMC8923215
OpenAlexW4206366284

What OpenQuestion holds

Textmetadata
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.