Evidence map›Paper›PMID 25500731›Full record

ArticleNature communications2014

MinCD cell division proteins form alternating copolymeric cytomotive filaments.

Debnath Ghosal, Daniel Trambaiolo, Linda A Amos, Jan Löwe

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Fast, StreamlinedChemical & biomedical imaging · 2026
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Distinct Morphological Fates of UropathogenicInfection and immunity · 2020
    Article
  14. C-terminal eYFP fusion impairsOpen biology · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The cell division protein MinD fromThe Journal of biological chemistry · 2018
    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 1 institution in 1 country.

Debnath GhosalStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Daniel TrambaioloStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Linda A AmosStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Jan LöweStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust 095514Wellcome Trust 095514/Z/11/Z
6 · The paper itself

Abstract

During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsBinding SitesCell Cycle ProteinsCell DivisionCell MembraneCrystallography, X-RayCytoskeletal ProteinsCytoskeletonEscherichia coliEscherichia coli ProteinsGene ExpressionGenes, ReporterGreen Fluorescent ProteinsLiposomesMembrane ProteinsAdenosine TriphosphatasesBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaGreen Fluorescent ProteinsLiposomesMembrane ProteinsMinC protein, E coliMinD protein, E coliMinE protein, E coliRecombinant Fusion Proteins

Identifiers

PMID25500731
PMCPMC4338524
OpenAlexW2100341083

What OpenQuestion holds

Textmetadata
LicenceTDM
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.