Evidence map›Paper›PMID 36123441›Full record

ArticleNature microbiology2022

Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.

Tim Nierhaus, Stephen H McLaughlin, Frank Bürmann, Danguole Kureisaite-Ciziene, Sarah L Maslen, J Mark Skehel, Conny W H Yu, Stefan M V Freund, Louise F H Funke, Jason W Chin and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Combining live fluorescence imaging with in situ cryoelectron tomography sheds light on the septation process inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. 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

11 authors at 1 institution in 1 country.

Tim NierhausMRC Laboratory of Molecular Biology, Cambridge, UK.
Stephen H McLaughlinMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0001-9135-6253
Frank BürmannMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0002-9428-0933
Danguole Kureisaite-CizieneMRC Laboratory of Molecular Biology, Cambridge, UK.
Sarah L MaslenMRC Laboratory of Molecular Biology, Cambridge, UK.
J Mark SkehelMRC Laboratory of Molecular Biology, Cambridge, UK.
Conny W H YuMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0002-6478-5762
Stefan M V FreundMRC Laboratory of Molecular Biology, Cambridge, UK.
Louise F H FunkeMRC Laboratory of Molecular Biology, Cambridge, UK.
Jason W ChinMRC Laboratory of Molecular Biology, Cambridge, UK.
Jan LöweMRC Laboratory of Molecular Biology, Cambridge, UK. jyl@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-5218-6615
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105181009Medical Research Council MC_U105184326Medical Research Council MC_UP_A024_1008Medical Research Council U105181009Medical Research Council U105184326Medical Research Council UPA0241008Wellcome Trust 202754Wellcome Trust 202754/Z/16/Z
6 · The paper itself

Abstract

During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA-FtsN interaction site in the IA-IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA-FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane.

Indexed as

Escherichia coliEscherichia coli ProteinsActinsBacterial ProteinsCysteineLipidsLiposomesMembrane ProteinsPeptidoglycanTubulinActinsBacterial ProteinsCysteineEscherichia coli ProteinsFtsA protein, E coliFtsN protein, E coliLipidsLiposomesMembrane ProteinsPeptidoglycanTubulin

Identifiers

PMID36123441
PMCPMC7613929
OpenAlexW4296293242

What Socratic holds

Textmetadata
LicenceCC BY
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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 Socratic graph.