Evidence map›Paper›PMID 34515361›Full record

ArticleThe EMBO journal2021

Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.

Marie-Louise R Francis, Melissa N Webby, Nicholas G Housden, Renata Kaminska, Emma Elliston, Boonyaporn Chinthammit, Natalya Lukoyanova, Colin Kleanthous

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

8 authors at 2 institutions in 1 country.

Marie-Louise R FrancisDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-4257-0162
Melissa N WebbyDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-5721-0381
Nicholas G HousdenDepartment of Biochemistry, University of Oxford, Oxford, UK.
Renata KaminskaDepartment of Biochemistry, University of Oxford, Oxford, UK.
Emma EllistonDepartment of Biochemistry, University of Oxford, Oxford, UK.
Boonyaporn ChinthammitDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-5433-7977
Natalya LukoyanovaDepartment of Biological Sciences, ISMB, Birkbeck College, London, UK.ORCID 0000-0002-2051-0812
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-3273-0302
University of Oxford · GBBirkbeck, University of London · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome TrustWellcome Trust 091911/B/10/ZWellcome Trust 107457/Z/15/ZWellcome Trust 201505/Z/16/ZWellcome Trust 202679/Z/16/ZWellcome Trust 206166/Z/17/Z
6 · The paper itself

Abstract

Bacteria deploy weapons to kill their neighbours during competition for resources and to aid survival within microbiomes. Colicins were the first such antibacterial system identified, yet how these bacteriocins cross the outer membrane (OM) of Escherichia coli is unknown. Here, by solving the structures of translocation intermediates via cryo-EM and by imaging toxin import, we uncover the mechanism by which the Tol-dependent nuclease colicin E9 (ColE9) crosses the bacterial OM. We show that threading of ColE9's disordered N-terminal domain through two pores of the trimeric porin OmpF causes the colicin to disengage from its primary receptor, BtuB, and reorganises the translocon either side of the membrane. Subsequent import of ColE9 through the lumen of a single OmpF subunit is driven by the proton-motive force, which is delivered by the TolQ-TolR-TolA-TolB assembly. Our study answers longstanding questions, such as why OmpF is a better translocator than OmpC, and reconciles the mechanisms by which both Tol- and Ton-dependent bacteriocins cross the bacterial outer membrane.

Indexed as

Bacterial Outer MembraneBacterial Outer Membrane ProteinsBacteriocinsBinding SitesColicinsCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialKineticsMembrane ProteinsMembrane Transport ProteinsModels, MolecularPeriplasmic ProteinsPorinsProtein BindingBacterial Outer Membrane ProteinsBacteriocinsBtuB protein, E coliColicinsEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsOmpF proteinPeriplasmic ProteinsPorinstolA protein, E colitolB protein, E colitolQ protein, E colitolR protein, E colibacteriocinscryo-electron microscopyfluorescent microscopyGram-negative bacteriaouter membrane

Identifiers

PMID34515361
PMCPMC8561637
OpenAlexW3199685002

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.