Evidence map›Paper›PMID 32161270›Full record

ArticleNature communications2020

The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.

Joanna Szczepaniak, Peter Holmes, Karthik Rajasekar, Renata Kaminska, Firdaus Samsudin, Patrick George Inns, Patrice Rassam, Syma Khalid, Seán M Murray, Christina Redfield and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Multiple TonB-dependent transport systems inInfection and immunity · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  12. Article
  13. Article
  14. Tissue-like structures formed by a bacterium.bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Autonomous division of the outer membrane in Gram-negative bacteria.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Rational Design of Natural Xanthones Against Gram-negative Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  19. Article
  20. Article

1 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

11 authors at 5 institutions in 4 countries.

Joanna Szczepaniak *Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0003-2441-6310
Peter Holmes *Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Karthik Rajasekar *Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Renata KaminskaDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Firdaus SamsudinDepartment of Chemistry, University of Southampton, University Road, Southampton, SO17 1BJ, UK.
Patrick George InnsDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Patrice RassamDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Syma KhalidDepartment of Chemistry, University of Southampton, University Road, Southampton, SO17 1BJ, UK.
Seán M MurrayMax Planck Institute for Terrestrial Microbiology and LOEWE Centre for Synthetic Microbiology (SYNMIKRO), Karl-von-Frisch Strasse 16, 35043, Marburg, Germany.ORCID http://orcid.org/0000-0002-2260-0774
Christina RedfieldDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0001-7297-7708
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK. colin.kleanthous@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0002-3273-0302
University of Oxford · GBUniversity of Southampton · GBCentre National de la Recherche Scientifique · FRPhilipps University of Marburg · DEUniversity of Alberta · CA

Funding

Medical Research CouncilWellcome TrustWellcome Trust 201505/Z/16/Z
6 · The paper itself

Abstract

Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.

Indexed as

Cell DivisionBacterial Outer MembraneBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsLipoproteinsMembrane ProteinsPeptidoglycanPeriplasmic ProteinsBacterial Outer Membrane ProteinsEscherichia coli ProteinsExcC protein, E coliLipoproteinsMembrane ProteinsPeptidoglycanPeriplasmic ProteinstolA protein, E colitolB protein, E colitolR protein, E coli

Identifiers

PMID32161270
PMCPMC7066135
OpenAlexW3010760226

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.