Evidence map›Paper›PMID 19346310›Full record

ArticleJournal of bacteriology2009

In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2.

Archana Varma, Kevin D Young

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 78 citations in OpenAlex.

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  13. Morphology engineering: a new strategy to construct microbial cell factories.World journal of microbiology & biotechnology · 2020
    Review
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  19. Bacterial Cell Size: Multifactorial and Multifaceted.Annual review of microbiology · 2017
    Review
  20. Article
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

2 authors at 1 institution in 1 country.

Archana VarmaDepartment of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota 58202-9037, USA.
Kevin D Young
University of North Dakota · US

Funding

Glycan Expression Analysis using an Odyssey CLx Infrared Imaging SystemR01GM061019 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VOTH, DANIEL E · 2000 to 2021
$8.0M
NIGMS NIH HHS R01 GM061019NIGMS NIH HHS R01-GM61019
6 · The paper itself

Abstract

In Escherichia coli, the cytoplasmic proteins MreB and FtsZ play crucial roles in ensuring that new muropeptide subunits are inserted into the cell wall in a spatially correct way during elongation and division. In particular, to retain a constant diameter and overall shape, new material must be inserted into the wall uniformly around the cell's perimeter. Current thinking is that MreB accomplishes this feat through intermediary proteins that tether peptidoglycan synthases to the outer face of the inner membrane. We tested this idea in E. coli by using a DD-carboxypeptidase mutant that accumulates pentapeptides in its peptidoglycan, allowing us to visualize new muropeptide incorporation. Surprisingly, inhibiting MreB with the antibiotic A22 did not result in uneven insertion of new wall, although the cells bulged and lost their rod shapes. Instead, uneven (clustered) incorporation occurred only if MreB and FtsZ were inactivated simultaneously, providing the first evidence in E. coli that FtsZ can direct murein incorporation into the lateral cell wall independently of MreB. Inhibiting penicillin binding protein 2 (PBP 2) alone produced the same clustered phenotype, implying that MreB and FtsZ tether peptidoglycan synthases via a common mechanism that includes PBP 2. However, cell shape was determined only by the presence or absence of MreB and not by the even distribution of new wall material as directed by FtsZ.

Indexed as

ArabinoseAztreonamBacterial ProteinsCell WallCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMicroscopy, ConfocalModels, BiologicalPenicillin-Binding ProteinsPeptidoglycanThiourea2,6-dichlorobenzylthiopseudoureaArabinoseAztreonamBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaMreB protein, E coliPenicillin-Binding ProteinsPeptidoglycansulA protein, E coliThiourea

Identifiers

PMID19346310
PMCPMC2681889
OpenAlexW2162328528

What OpenQuestion holds

Textmetadata
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.