Evidence map›Paper›PMID 19666716›Full record

ArticleJournal of bacteriology2009

Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli lipid II flippase, are not essential for growth.

Allison Fay, Jonathan Dworkin

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Journal of bacteriology · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. GtcA is required for LTA glycosylation inCell surface (Amsterdam, Netherlands) · 2020
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. MurJ and a novel lipid II flippase are required for cell wall biogenesis in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Review
  15. Spore formation in Bacillus subtilis.Environmental microbiology reports · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Bacterial cell-wall recycling.Annals of the New York Academy of Sciences · 2013
    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

2 authors at 1 institution in 1 country.

Allison FayDepartment of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Jonathan Dworkin
Columbia University · US

Funding

TRAINING PROGRAM IN MICROBIOLOGY FOR INFECTIOUS DISEASEST32AI007161 · NIAID · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI FIDOCK, DAVID A · 1985 to 2008
$1.9M
Peptidoglycan synthesis during sporulationR01GM081368 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI DWORKIN, JONATHAN · 2008 to 2012
$1.6M
NIAID NIH HHS T32 AI007161NIAID NIH HHS T32AI07161-29NIGMS NIH HHS R01 GM081368NIGMS NIH HHS R01GM081368-01
6 · The paper itself

Abstract

Although peptidoglycan synthesis is one of the best-studied metabolic pathways in bacteria, the mechanism underlying the membrane translocation of lipid II, the undecaprenyl-disaccharide pentapeptide peptidoglycan precursor, remains mysterious. Recently, it was proposed that the essential Escherichia coli mviN gene encodes the lipid II flippase. Bacillus subtilis contains four proteins that are putatively homologous to MviN, including SpoVB, previously reported to be necessary for spore cortex peptidoglycan synthesis during sporulation. MviN complemented the sporulation defect of a DeltaspoVB mutation, and SpoVB and another of the B. subtilis homologs, YtgP, complemented the growth defect of an E. coli strain depleted for MviN. Thus, these B. subtilis proteins are likely to be MviN homologs. However, B. subtilis strains lacking these four proteins have no defects in growth, indicating that they likely do not serve as lipid II flippases in this organism.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsComputational BiologyEscherichia coli ProteinsGenetic Complementation TestMembrane ProteinsMicroscopy, FluorescenceMolecular Sequence DataPeptidoglycanSequence Homology, Amino AcidUridine Diphosphate N-Acetylmuramic AcidBacterial ProteinsEscherichia coli ProteinsMembrane Proteinsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolPeptidoglycanSpoVB protein, BacillusUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID19666716
PMCPMC2747889
OpenAlexW2124411207

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.