Evidence map›Paper›PMID 30230648›Full record

ArticleMolecular microbiology2018

Cell cycle-dependent regulation of FtsZ in Escherichia coli in slow growth conditions.

Jaana Männik, Bryant E Walker, Jaan Männik

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
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  7. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
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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

3 authors at 1 institution in 1 country.

Jaana MännikDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, 37996, USA.ORCID 0000-0002-0777-7846
Bryant E WalkerDepartment of Physics and Astronomy, University of Tennessee, Knoxville, TN, 37996, USA.
Jaan MännikDepartment of Physics and Astronomy, University of Tennessee, Knoxville, TN, 37996, USA.ORCID 0000-0002-6759-3053
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
Basic Energy SciencesNational Science Foundation 1252890NIGMS NIH HHS R01 GM127413NIH HHS R01GM127413NSF 1252890Oak Ridge National LaboratoryOffice of Basic Energy Sciences, U.S. Department of EnergyUniversity of TennesseeU.S. Department of EnergyUS-Israel Binational Science Foundation 2017004US-Israel BSF 2017004
6 · The paper itself

Abstract

FtsZ is the key regulator of bacterial cell division. It initiates division by forming a dynamic ring-like structure, the Z-ring, at the mid-cell. What triggers the formation of the Z-ring during the cell cycle is poorly understood. In Escherichia coli, the common view is that FtsZ concentration is constant throughout its doubling time and therefore regulation of assembly is controlled by some yet-to-be-identified protein-protein interactions. Using a newly developed functional, fluorescent FtsZ reporter, we performed a quantitative analysis of the FtsZ concentration throughout the cell cycle under slow growth conditions. In contrast to the common expectation, we show that FtsZ concentrations vary in a cell cycle-dependent manner, and that upregulation of FtsZ synthesis correlates with the formation of the Z-ring. The first half of the cell cycle shows an approximately fourfold upregulation of FtsZ synthesis, followed by its rapid degradation by ClpXP protease in the last 10% of the cell cycle. The initiation of rapid degradation coincides with the dissociation of FtsZ from the septum. Altogether, our data suggest that the Z-ring formation in slow growth conditions in E. coli is partially controlled by a regulatory sequence wherein upregulation of an essential cell cycle factor is followed by its degradation.

Indexed as

Cell DivisionBacterial ProteinsCell Cycle CheckpointsCell Cycle ProteinsCytoskeletal ProteinsEndopeptidase ClpEscherichia coliEscherichia coli ProteinsProtein BindingBacterial ProteinsCell Cycle ProteinsClpXP protease, E coliCytoskeletal ProteinsEndopeptidase ClpEscherichia coli ProteinsFtsZ protein, Bacteria

Identifiers

PMID30230648
PMCPMC6311098
OpenAlexW2890590861

What OpenQuestion holds

Textmetadata
LicenceTDM
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.