Evidence map›Paper›PMID 15466028›Full record

ArticleJournal of bacteriology2004

FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli.

Archana Varma, Kevin D Young

Abstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Morphology engineering: a new strategy to construct microbial cell factories.World journal of microbiology & biotechnology · 2020
    Review
  5. Bacterial cell division at a glance.Journal of cell science · 2020
    Review
  6. Article
  7. Emergence ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. HflX protein protectsJournal of biosciences · 2018
    Article
  9. Review
  10. Article
  11. Frontiers in microbiology · 2017
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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, ND 58202, USA. kyoung@medicine.nodak.edu.
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

The mechanisms by which bacteria adopt and maintain individual shapes remain enigmatic. Outstanding questions include why cells are a certain size, length, and width; why they are uniform or irregular; and why some branch while others do not. Previously, we showed that Escherichia coli mutants lacking multiple penicillin binding proteins (PBPs) display extensive morphological diversity. Because defective sites in these cells exhibit the structural and functional characteristics of improperly localized poles, we investigated the connection between cell division and shape. Here we show that under semipermissive conditions the temperature-sensitive FtsZ84 protein produces branched and aberrant cells at a high frequency in mutants lacking PBP 5, and this phenotype is exacerbated by the loss of additional peptidoglycan endopeptidases. Surprisingly, certain ftsZ84 strains lyse at the nonpermissive temperature instead of filamenting, and inhibition of wild-type FtsZ forces some mutants into tightly wound spirillum-like morphologies. The results demonstrate that significant aspects of bacterial shape are dictated by a previously unrecognized relationship between the septation machinery and ostensibly minor peptidoglycan-modifying enzymes and that under certain circumstances improper FtsZ function can destroy the structural integrity of the cell.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBacteriolysisCarrier ProteinsEscherichia coliEscherichia coli ProteinsHexosyltransferasesMicroscopy, Electron, ScanningMuramoylpentapeptide CarboxypeptidaseMutagenesis, Site-DirectedMutationPenicillin-Binding ProteinsPeptidyl TransferasesBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsFtsZ84 protein, E coliHexosyltransferasesMuramoylpentapeptide CarboxypeptidasePenicillin-Binding ProteinsPeptidyl Transferases

Identifiers

PMID15466028
PMCPMC522200
OpenAlexW2101043542

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.