Evidence map›Paper›PMID 25423369›Full record

ArticleBioscience reports2015

Structural characterization of the late competence protein ComFB from Bacillus subtilis.

Tatyana A Sysoeva, Lukas B Bane, Daphne Y Xiao, Baundauna Bose, Scott S Chilton, Rachelle Gaudet, Briana M Burton

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. 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
  2. Article
  3. c-di-GMP-Dependent Regulation of Motility bybioRxiv : the preprint server for biology · 2025
    Article
  4. ComFB, a new widespread family of c-di-NMP receptor proteins.bioRxiv : the preprint server for biology · 2024
    Article
  5. A c-di-GMP binding effector controls cell size in a cyanobacterium.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Testing the retroelement invasion hypothesis for the emergence of the ancestral eukaryotic cell.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. 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

7 authors at 1 institution in 1 country.

Tatyana A Sysoeva*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Lukas B Bane*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Daphne Y Xiao*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Baundauna Bose*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Scott S Chilton*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Rachelle Gaudet*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Briana M Burton*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, U.S.A.
Harvard University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Many bacteria take up DNA from their environment as part of the process of natural transformation. DNA uptake allows microorganisms to gain genetic diversity and can lead to the spread of antibiotic resistance or virulence genes within a microbial population. Development of genetic competence (Com) in Bacillus subtilis is a highly regulated process that culminates in expression of several late competence genes and formation of the DNA uptake apparatus. The late competence operon comF encodes a small protein of unknown function, ComFB. To gain insight into the function of ComFB, we determined its 3D structure via X-ray crystallography. ComFB is a dimer and each subunit consists of four α-helices connected by short loops and one extended β-strand-like stretch. Each subunit contains one zinc-binding site formed by four cysteines, which are unusually spaced in the primary sequence. Using structure- and bioinformatics-guided substitutions we analyzed the inter-subunit interface of the ComFB dimer. Based on these analyses, we conclude that ComFB is an obligate dimer. We also characterized ComFB in vivo and found that this protein is produced in competent cells and is localized to the cytosol. Consistent with previous reports, we showed that deletion of ComFB does not affect DNA uptake function. Combining our results, we conclude that ComFB is unlikely to be a part of the DNA uptake machinery under tested conditions and instead may have a regulatory function.

Indexed as

Protein MultimerizationBacillus subtilisBacterial ProteinsCrystallography, X-RayProtein Structure, QuaternaryProtein Structure, SecondaryStructure-Activity RelationshipBacterial Proteins

Identifiers

PMID25423369
PMCPMC4381287
OpenAlexW2021250663

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.