Evidence map›Paper›PMID 25496050›Full record

ArticleMolecular microbiology2015

A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.

Mary-Jane Tsang, Thomas G Bernhardt

Abstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed.

  1. Article
  2. Defining the order of assembly of theJournal of bacteriology · 2026
    Article
  3. Article
  4. Article
  5. Control of cell division by anbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026
    Article
  8. A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Control of morphogenesis during theScience advances · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

39 more citing papers are in PubMed but not listed here.

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.

Mary-Jane TsangDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.
Thomas G Bernhardt

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Identifying and validating new antibiotic targets in cell wall synthesis pathwaysR01AI099144 · NIAID · HARVARD MEDICAL SCHOOL · PI BERNHARDT, THOMAS G, WALKER, SUZANNE · 2012 to 2016
$4.3M
NIAID NIH HHS R01 AI083365NIAID NIH HHS R01 AI099144
6 · The paper itself

Abstract

The cytokinetic apparatus of bacteria is initially formed by the polymerization of the tubulin-like FtsZ protein into a ring structure at midcell. This so-called Z-ring facilitates the recruitment of many additional proteins to the division site to form the mature divisome machine. Although the assembly pathway leading to divisome formation has been well characterized, the mechanisms that trigger cell constriction remain unclear. In this report, we study a 'forgotten' allele of ftsL from Escherichia coli, which encodes a conserved division gene of unknown function. We discovered that this allele promotes the premature initiation of cell division. Further analysis also revealed that the mutant bypasses the requirement for the essential division proteins ZipA, FtsK and FtsN, and partially bypasses the need for FtsA. These findings suggest that rather than serving simply as a protein scaffold within the divisome, FtsL may play a more active role in the activation of the machine. Our results support a model in which FtsL, along with its partners FtsB and FtsQ, function as part of a sensing mechanism that promotes the onset of cell wall remodeling processes needed for the initiation of cell constriction once assembly of the divisome complex is deemed complete.

Indexed as

Cell DivisionAllelesCarrier ProteinsCell Cycle ProteinsCell WallCytokinesisEscherichia coliEscherichia coli ProteinsMembrane ProteinsMutationCarrier ProteinsCell Cycle ProteinsEscherichia coli ProteinsFtsB protein, E coliftsL protein, E coliFtsQ protein, E coliMembrane ProteinsZipA protein, E coli

Identifiers

PMID25496050
PMCPMC4414402

What OpenQuestion holds

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Registered trials

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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.