Evidence map›Paper›PMID 25848771›Full record

ArticlePLoS genetics2015

A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.

Jackson Buss, Carla Coltharp, Gleb Shtengel, Xinxing Yang, Harald Hess, Jie Xiao

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
14.8field-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

71 citing papers in PubMed, 119 citations in OpenAlex.

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  15. mBio · 2022
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  20. Article

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

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

6 authors at 3 institutions in 1 country.

Jackson BussDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Carla ColtharpDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Gleb ShtengelJanelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia, United States of America.
Xinxing YangDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Harald HessJanelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia, United States of America.
Jie XiaoDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Janelia Research Campus · USJohns Hopkins Medicine · USJohns Hopkins University · US

Funding

Probing the structure, dynamics and function of the E. coli divisomeR01GM086447 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI XIAO, JIE · 2011 to 2019
$3.8M
NIGMS NIH HHS 1R01GM08644715 01A2NIGMS NIH HHS R01 GM086447
6 · The paper itself

Abstract

The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. The FtsZ-ring establishes the division plane and enables the assembly of the macromolecular division machinery (divisome). Although many molecular components of the divisome have been identified and their interactions extensively characterized, the spatial organization of these proteins within the divisome is unclear. Consequently, the physical mechanisms that drive divisome assembly, maintenance, and constriction remain elusive. Here we applied single-molecule based superresolution imaging, combined with genetic and biophysical investigations, to reveal the spatial organization of cellular structures formed by four important divisome proteins in E. coli: FtsZ, ZapA, ZapB and MatP. We show that these interacting proteins are arranged into a multi-layered protein network extending from the cell membrane to the chromosome, each with unique structural and dynamic properties. Further, we find that this protein network stabilizes the FtsZ-ring, and unexpectedly, slows down cell constriction, suggesting a new, unrecognized role for this network in bacterial cell division. Our results provide new insight into the structure and function of the divisome, and highlight the importance of coordinated cell constriction and chromosome segregation.

Indexed as

Cell DivisionBacterial ProteinsCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMotionBacterial ProteinsCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaMatP protein, E coliZapA protein, E coliZapB protein, E coli

Identifiers

PMID25848771
PMCPMC4388696
OpenAlexW2095995504

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.