Evidence map›Paper›PMID 25496160›Full record

ArticleMolecular microbiology2015

Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.

Bing Liu, Logan Persons, Lynda Lee, Piet A J de Boer

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 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing 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

122 citing papers in PubMed.

  1. Defining the order of assembly of theJournal of bacteriology · 2026
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  7. Control of cell division by anbioRxiv : the preprint server for biology · 2026
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  9. Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026
    Article
  10. 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
  11. Article
  12. FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
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62 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

4 authors.

Bing LiuDepartment of Molecular Biology & Microbiology, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106-4960, USA.
Logan Persons
Lynda Lee
Piet A J de Boer

Funding

ASSEMBLY AND FUNCTION OF THE SEPTAL RING IN E COLIR01GM057059 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI DE BOER, PIET A · 1998 to 2016
$5.1M
NIGMS NIH HHS NIH GM57059NIGMS NIH HHS R01 GM057059
6 · The paper itself

Abstract

Escherichia coli FtsN is a bitopic membrane protein that is essential for triggering active cell constriction. A small periplasmic subdomain ((E) FtsN) is required and sufficient for function, but its mechanism of action is unclear. We isolated extragenic (E) FtsN*-suppressing mutations that restore division in cells producing otherwise non-functional variants of FtsN. These mapped to the IC domain of FtsA in the cytoplasm and to small subdomains of the FtsB and FtsL proteins in the periplasm. All FtsB and FtsL variants allowed survival without (E) FtsN, but many then imposed a new requirement for interaction between the cytoplasmic domain of FtsN ((N) FtsN) and FtsA. Alternatively, variants of FtsA, FtsB or FtsL acted synergistically to allow cell division in the complete absence of FtsN. Strikingly, moreover, substitution of a single residue in FtsB (E56) proved sufficient to rescue ΔftsN cells as well. In FtsN(+) cells, (E) FtsN*-suppressing mutations promoted cell fission at an abnormally small cell size, and caused cell shape and integrity defects under certain conditions. This and additional evidence support a model in which FtsN acts on either side of the membrane to induce a conformational switch in both FtsA and the FtsBLQ subcomplex to de-repress septal peptidoglycan synthesis and membrane invagination.

Indexed as

Cell DivisionAmino Acid SubstitutionCell Cycle ProteinsCell WallEscherichia coliEscherichia coli ProteinsMembrane ProteinsMicrobial ViabilityModels, BiologicalMutationPhylogenySuppression, GeneticCell Cycle ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsB protein, E coliftsL protein, E coliFtsN protein, E coliFtsQ protein, E coliMembrane Proteins

Identifiers

PMID25496160
PMCPMC4428282

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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.