Evidence map›Paper›PMID 31978334›Full record

ArticleCurrent biology : CB2020

Transient Membrane-Linked FtsZ Assemblies Precede Z-Ring Formation in Escherichia coli.

Bryant E Walker, Jaana Männik, Jaan Männik

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.3field-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

19 citing papers in PubMed, 39 citations in OpenAlex.

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  12. FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  15. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Bryant E WalkerDepartment of Physics and Astronomy, University of Tennessee, Knoxville, TN 37996, USA.
Jaana MännikDepartment of Physics and Astronomy, University of Tennessee, Knoxville, TN 37996, USA; Department of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Jaan MännikDepartment of Physics and Astronomy, University of Tennessee, Knoxville, TN 37996, USA. Electronic address: jmannik@utk.edu.
University of Tennessee at Knoxville · US

Funding

Coordination mechanisms between cell division and chromosome segregation in E. coliR01GM127413 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI Jaan Mannik · 2018 to 2026
$2.5M
NIGMS NIH HHS R01 GM127413
6 · The paper itself

Abstract

During the early stages of cytokinesis, FtsZ protofilaments form a ring-like structure, the Z-ring, in most bacterial species. This cytoskeletal scaffold recruits downstream proteins essential for septal cell wall synthesis. Despite progress in understanding the dynamic nature of the Z-ring and its role in coordinating septal cell wall synthesis, the early stages of protofilament formation and subsequent assembly into the Z-ring are still not understood. Here we investigate a sequence of assembly steps that lead to the formation of the Z-ring in Escherichia coli using high temporal and spatial resolution imaging. Our data show that formation of the Z-ring is preceded by transient membrane-linked FtsZ assemblies. These assemblies form after attachment of short cytosolic protofilaments, which we estimate to be less than 20 monomers long, to the membrane. The attachments occur at random locations along the length of the cell. The filaments treadmill and show periods of rapid growth and shrinkage. Their dynamic properties imply that protofilaments are bundled in these assemblies. Furthermore, we establish that the size of assemblies is sensitively controlled by the availability of FtsZ molecules and by the presence of ZapA proteins. The latter has been implicated in cross-linking the protofilaments. The likely function of these dynamic FtsZ assemblies is to sample the cell surface for the proper location for the Z-ring.

Indexed as

Bacterial ProteinsCytokinesisCytoskeletal ProteinsCytoskeletonEscherichia coliEscherichia coli ProteinsBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, Bacteriacell divisionEscherichia coliFtsZmother machineprotofilament self-assemblyZ-ring

Identifiers

PMID31978334
PMCPMC7190073
OpenAlexW3002464534

What OpenQuestion holds

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Registered trials

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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.