Evidence map›Paper›PMID 17513471›Full record

ArticleJournal of bacteriology2007

FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli.

Archana Varma, Miguel A de Pedro, Kevin D Young

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Cardiolipin AltersmBio · 2019
    Article
  7. Bacterial Cell Size: Multifactorial and Multifaceted.Annual review of microbiology · 2017
    Review
  8. Article
  9. Article
  10. Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  11. Frontiers in microbiology · 2017
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Targeting the Bacterial Division Protein FtsZ.Journal of medicinal chemistry · 2016
    Review
  17. Article
  18. Defining the rate-limiting processes of bacterial cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Mechanisms of bacterial morphogenesis: evolutionary cell biology approaches provide new insights.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Article
  20. Review
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.

Archana VarmaDepartment of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202, USA.
Miguel A de Pedro
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 GM61019NIGMS NIH HHS R01 GM061019
6 · The paper itself

Abstract

Certain penicillin binding protein mutants of Escherichia coli grow with spirillum-like morphologies when the FtsZ protein is inhibited, suggesting that FtsZ might govern aspects of cell wall growth other than those strictly associated with septation. While investigating the mechanism of spiral cell formation, we discovered conditions for visualizing this second function of FtsZ. Normally, inhibiting the cytoskeleton protein MreB forces E. coli cells to grow as smoothly enlarging spheres from which the poles disappear, yielding coccoid or lemon-shaped forms. However, when FtsZ and MreB were inhibited simultaneously in a strain lacking PBP 5 and PBP 7, the resulting cells ballooned outward but retained conspicuous rod-shaped extensions at sites representing the original poles. This visual phenotype was paralleled by the biochemistry of sacculus growth. Muropeptides are usually inserted homogeneously into the lateral cell walls, but when FtsZ polymerization was inhibited, the incorporation of new material occurred mainly in the central regions of cells and was significantly lower in those portions of side walls abutting a pole. Thus, reduced precursor incorporation into side walls near the poles explained why these regions retained their rod-like morphology while the rest of the cell grew spherically. Also, inhibiting FtsZ increased the amount of pentapeptides in sacculi by about one-third. Finally, the MreB protein directed the helical or diagonal incorporation of new peptidoglycan into the wall, but the location of that incorporation depended on whether FtsZ was active. In sum, the results indicate that in addition to nucleating cell septation in E. coli, FtsZ can direct the insertion of new peptidoglycan into portions of the lateral wall.

Indexed as

Cell WallEscherichia coliEscherichia coli ProteinsMicroscopy, ConfocalMicroscopy, Phase-ContrastPeptidoglycanEscherichia coli ProteinsFtsZ84 protein, E coliMreB protein, E coliPeptidoglycan

Identifiers

PMID17513471
PMCPMC1951832
OpenAlexW2169946764

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.