Evidence map›Paper›PMID 30504892›Full record

ArticleNature communications2018

Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division.

Manuel Pazos, Katharina Peters, Mercedes Casanova, Pilar Palacios, Michael VanNieuwenhze, Eefjan Breukink, Miguel Vicente, Waldemar Vollmer

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
–field-weighted citation impact
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

46 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Manuel PazosCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Katharina PetersCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Mercedes CasanovaCentro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.
Pilar PalaciosCentro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.
Michael VanNieuwenhzeMolecular and Cellular Biochemistry Department, Biology Department, Indiana University, 212S. Hawthorne Dr, Bloomington, IN, 47405, USA.ORCID http://orcid.org/0000-0001-6093-5949
Eefjan BreukinkMembrane Biochemistry and Biophysics, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-7311-0660
Miguel VicenteCentro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Darwin 3, 28049, Madrid, Spain.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK. w.vollmer@ncl.ac.uk.

Funding

Dynamics of bacterial peptidoglycan synthesisR01GM113172 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V, VANNIEUWENHZE, MICHAEL S · 2015 to 2018
$3.5M
Novel Inhibitors of Peptidoglycan Biosynthesis Targeting Gram-positive PathogensR01GM111537 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI VANNIEUWENHZE, MICHAEL S · 2014 to 2017
$1.4M
Medical Research Council MR/N002679/1NIGMS NIH HHS R01 GM111537NIGMS NIH HHS R01 GM113172Wellcome Trust
6 · The paper itself

Abstract

During the transition from elongation to septation, Escherichia coli establishes a ring-like peptidoglycan growth zone at the future division site. This preseptal peptidoglycan synthesis does not require the cell division-specific peptidoglycan transpeptidase PBP3 or most of the other cell division proteins, but it does require FtsZ, its membrane-anchor ZipA and at least one of the bi-functional transglycosylase-transpeptidases, PBP1A or PBP1B. Here we show that PBP1A and PBP1B interact with ZipA and localise to preseptal sites in cells with inhibited PBP3. ZipA stimulates the glycosyltransferase activity of PBP1A. The membrane-anchored cell division protein FtsN localises at preseptal sites and stimulates both activities of PBP1B. Genes zipA and ftsN can be individually deleted in ftsA* mutant cells, but the simultaneous depletion of both proteins is lethal and cells do not establish preseptal sites. Our data support a model according to which ZipA and FtsN-FtsA have semi-redundant roles in connecting the cytosolic FtsZ ring with the membrane-anchored peptidoglycan synthases during the preseptal phase of envelope growth.

Indexed as

Bacterial ProteinsCell DivisionCell WallEscherichia coli ProteinsGlycosyltransferasesPeptidoglycanBacterial ProteinsEscherichia coli ProteinsGlycosyltransferasesPeptidoglycan

Identifiers

PMID30504892
PMCPMC6269477

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.