Evidence map›Paper›PMID 26517549›Full record

ArticlePloS one2015

Bacillus subtilis Bactofilins Are Essential for Flagellar Hook- and Filament Assembly and Dynamically Localize into Structures of Less than 100 nm Diameter underneath the Cell Membrane.

Jihad El Andari, Florian Altegoer, Gert Bange, Peter L Graumann

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Discovery of Coerumycin, a Cinnamycin-like Lantibiotic fromAntibiotics (Basel, Switzerland) · 2026
    Article
  3. DUF4004 protein BacR (YhbD) ofFrontiers in microbiology · 2026
    Article
  4. Article
  5. Article
  6. Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Distinct regions ofeLife · 2022
    Article
  8. Article
  9. Insights Into the Helical Shape Complex ofFrontiers in microbiology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 3 institutions in 1 country.

Jihad El AndariSYNMIKRO, LOEWE Center for Synthetic Microbiology, and Department of Chemistry, Philipps Universität Marburg, Marburg, Germany; University of Freiburg, Faculty of Biology, Schaenzlestrasse 1, D-79104, Freiburg, Germany.
Florian AltegoerSYNMIKRO, LOEWE Center for Synthetic Microbiology, and Department of Chemistry, Philipps Universität Marburg, Marburg, Germany.
Gert BangeSYNMIKRO, LOEWE Center for Synthetic Microbiology, and Department of Chemistry, Philipps Universität Marburg, Marburg, Germany.
Peter L GraumannSYNMIKRO, LOEWE Center for Synthetic Microbiology, and Department of Chemistry, Philipps Universität Marburg, Marburg, Germany.
Loewe Center for Synthetic Microbiology · DEPhilipps University of Marburg · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bactofilins are a widely conserved protein family implicated in cell shape maintenance and in bacterial motility. We show that the bactofilins BacE and BacF from Bacillus subtilis are essential for motility. The proteins are required for the establishment of flagellar hook- and filament structures, but apparently not for the formation of basal bodies. Functional YFP fusions to BacE and to BacF localize as discrete assemblies at the B. subtilis cell membrane, and have a diameter of 60 to 70 nm. BacF assemblies are relatively static, and partially colocalize with flagellar basal bodies, while BacE assemblies are fewer per cell than those of BacF and are highly mobile. Tracking of BacE foci showed that the assemblies arrest at a single point for a few hundred milliseconds, showing that a putative interaction with flagellar structures would be transient and fast. When overexpressed or expressed in a heterologous cell system, bactofilins can form filamentous structures, and also form multimers as purified proteins. Our data reveal a propensity for bactofilins to form filaments, however, in B. subtilis cells, bactofilins assemble into defined size assemblies that show a dynamic localization pattern and play a role in flagellar assembly.

Indexed as

AnimalsBacillus subtilisBacterial ProteinsCell LineCell MembraneDNA, BacterialDrosophila melanogasterEscherichia coliFlagellaGenes, ReporterLuminescent ProteinsMotionRecombinant Fusion ProteinsTransfectionTransformation, BacterialBacterial ProteinsDNA, BacterialLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID26517549
PMCPMC4627819
OpenAlexW1944421329

What OpenQuestion holds

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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.