Evidence map›Paper›PMID 28695917›Full record

ArticleNature communications2017

Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.

Marcin Krupka, Veronica W Rowlett, Dustin Morado, Heidi Vitrac, Kara Schoenemann, Jun Liu, William Margolin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.5field-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

43 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  8. Review
  9. Article
  10. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  11. Review
  12. Article
  13. Article
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  15. Article
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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.

Marcin KrupkaDepartment of Microbiology and Molecular Genetics, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.
Veronica W RowlettDepartment of Microbiology and Molecular Genetics, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.ORCID 0000-0001-9232-9281
Dustin MoradoDepartment of Pathology and Laboratory Medicine, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.
Heidi VitracDepartment of Biochemistry and Molecular Biology, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.
Kara SchoenemannDepartment of Microbiology and Molecular Genetics, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.ORCID 0000-0001-6021-8325
Jun LiuDepartment of Pathology and Laboratory Medicine, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.
William MargolinDepartment of Microbiology and Molecular Genetics, McGovern Medical School, 6431 Fannin Street, Houston, Texas 77030, USA.
The University of Texas Health Science Center · US

Funding

Targeting and assembly of E. coli division proteinsR01GM061074 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MARGOLIN, WILLIAM · 2000 to 2018
$5.7M
Structural basis of signaling between bacterial chemoreceptors and flagellaR01GM107629 · NIGMS · YALE UNIVERSITY · PI LIU, JUN · 2014 to 2017
$1.5M
NIGMS NIH HHS R01 GM061074NIGMS NIH HHS R01 GM107629
6 · The paper itself

Abstract

Most bacteria divide using a protein machine called the divisome that spans the cytoplasmic membrane. Key divisome proteins on the membrane's cytoplasmic side include tubulin-like FtsZ, which forms GTP-dependent protofilaments, and actin-like FtsA, which tethers FtsZ to the membrane. Here we present genetic evidence that in Escherichia coli, FtsA antagonizes FtsZ protofilament bundling in vivo. We then show that purified FtsA does not form straight polymers on lipid monolayers as expected, but instead assembles into dodecameric minirings, often in hexameric arrays. When coassembled with FtsZ on lipid monolayers, these FtsA minirings appear to guide FtsZ to form long, often parallel, but unbundled protofilaments, whereas a mutant of FtsZ (FtsZ*) with stronger lateral interactions remains bundled. In contrast, a hypermorphic mutant of FtsA (FtsA*) forms mainly arcs instead of minirings and enhances lateral interactions between FtsZ protofilaments. Based on these results, we propose that FtsA antagonizes lateral interactions between FtsZ protofilaments, and that the oligomeric state of FtsA may influence FtsZ higher-order structure and divisome function.

Indexed as

Bacterial ProteinsCell MembraneCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsLipid BilayersLipidsProtein BindingBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaLipid BilayersLipids

Identifiers

PMID28695917
PMCPMC5508204
OpenAlexW2734777396

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.