Evidence map›Paper›PMID 32866331›Full record

ArticleMolecular microbiology2020

Cell division is antagonized by the activity of peptidoglycan endopeptidases that promote cell elongation.

Thao T Truong, Andrea Vettiger, Thomas G Bernhardt

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. mBio · 2026
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  9. Review
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  12. Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Article
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  19. Transposon insertion site sequencing (TIS) of Pseudomonas aeruginosa.Journal of microbiology (Seoul, Korea) · 2021
    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

3 authors at 2 institutions in 1 country.

Thao T TruongDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Andrea VettigerDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Thomas G BernhardtDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0003-3566-7756
Harvard University · USHoward Hughes Medical Institute · US

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Fluorescence Microscope for Time-Lapse Imaging of BacteriaS10RR027344 · NCRR · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2010 to 2010
$162k
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR027344NIAID NIH HHS R01 AI083365
6 · The paper itself

Abstract

A peptidoglycan (PG) cell wall composed of glycans crosslinked by short peptides surrounds most bacteria and protects them against osmotic rupture. In Escherichia coli, cell elongation requires crosslink cleavage by PG endopeptidases to make space for the incorporation of new PG material throughout the cell cylinder. Cell division, on the contrary, requires the localized synthesis and remodeling of new PG at midcell by the divisome. Little is known about the factors that modulate transitions between these two modes of PG biogenesis. In a transposon-insertion sequencing screen to identify mutants synthetically lethal with a defect in the division protein FtsP, we discovered that mutants impaired for cell division are sensitive to elevated activity of the endopeptidases. Increased endopeptidase activity in these cells was shown to interfere with the assembly of mature divisomes, and conversely, inactivation of MepS was found to suppress the lethality of mutations in essential division genes. Overall, our results are consistent with a model in which the cell elongation and division systems are in competition with one another and that control of PG endopeptidase activity represents an important point of regulation influencing the transition from elongation to the division mode of PG biogenesis.

Indexed as

Cell DivisionCell WallCysteine EndopeptidasesEndopeptidasesEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialMutationPeptidoglycanCysteine EndopeptidasesEndopeptidasesEscherichia coli ProteinsmepS protein, E coliPeptidoglycanpeptidoglycan endopeptidasecell divisioncell wallcytokinesiselongationmorphogenesispeptidoglycan

Identifiers

PMID32866331
PMCPMC7775348
OpenAlexW3081673076

What OpenQuestion holds

Textmetadata
LicenceTDM
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.