Evidence map›Paper›PMID 22473211›Full record

ArticleThe EMBO journal2012

FtsA forms actin-like protofilaments.

Piotr Szwedziak, Qing Wang, Stefan M V Freund, Jan Löwe

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
12.0field-weighted citation impact, top 1% 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

137 citing papers in PubMed, 244 citations in OpenAlex.

  1. Article
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  9. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA.International journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

77 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Piotr SzwedziakMRC Laboratory of Molecular Biology, Cambridge, UK.
Qing Wang
Stefan M V Freund
Jan Löwe
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326Medical Research Council U105184326
6 · The paper itself

Abstract

FtsA is an early component of the Z-ring, the structure that divides most bacteria, formed by tubulin-like FtsZ. FtsA belongs to the actin family of proteins, showing an unusual subdomain architecture. Here we reconstitute the tethering of FtsZ to the membrane via FtsA's C-terminal amphipathic helix in vitro using Thermotoga maritima proteins. A crystal structure of the FtsA:FtsZ interaction reveals 16 amino acids of the FtsZ tail bound to subdomain 2B of FtsA. The same structure and a second crystal form of FtsA reveal that FtsA forms actin-like protofilaments with a repeat of 48 Å. The identical repeat is observed when FtsA is polymerized using a lipid monolayer surface and FtsAs from three organisms form polymers in cells when overexpressed, as observed by electron cryotomography. Mutants that disrupt polymerization also show an elongated cell division phenotype in a temperature-sensitive FtsA background, demonstrating the importance of filament formation for FtsA's function in the Z-ring.

Indexed as

Bacterial ProteinsCrystallography, X-RayCytoskeletal ProteinsMicroscopy, ElectronModels, BiologicalModels, MolecularProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryThermotoga maritimaBacterial ProteinsCytoskeletal ProteinsFtsA protein, BacteriaFtsZ protein, Bacteria

Identifiers

PMID22473211
PMCPMC3364754
OpenAlexW2144743370

What OpenQuestion holds

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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.