Evidence map›Paper›PMID 26538516›Full record

ArticleMolecular microbiology2016

Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C-ring assembly in T3SS.

Melanie A McDowell, Julien Marcoux, Gareth McVicker, Steven Johnson, Yu Hang Fong, Rebecca Stevens, Lesley A H Bowman, Matteo T Degiacomi, Jun Yan, Adam Wise and 6 more

Abstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
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  14. Toward aInternational journal of molecular sciences · 2023
    Review
  15. Differential regulation ofFrontiers in cellular and infection microbiology · 2023
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. TheMicroorganisms · 2021
    Review
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

16 authors.

Melanie A McDowellSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Julien MarcouxDepartment of Chemistry, University of Oxford, Oxford, UK.
Gareth McVickerSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Steven JohnsonSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Yu Hang FongSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Rebecca StevensSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Lesley A H BowmanSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Matteo T DegiacomiDepartment of Chemistry, University of Oxford, Oxford, UK.
Jun YanDepartment of Chemistry, University of Oxford, Oxford, UK.
Adam WiseSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Miriam E FriedeSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Justin L P BeneschDepartment of Chemistry, University of Oxford, Oxford, UK.
Janet E DeaneSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Christoph M TangSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford, UK.
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Funding

Medical Research Council G0900888Medical Research Council M011984Medical Research Council MR/M011984/1Wellcome Trust 083599Wellcome Trust 100140Wellcome Trust 100298Wellcome Trust 102908
6 · The paper itself

Abstract

Flagellar type III secretion systems (T3SS) contain an essential cytoplasmic-ring (C-ring) largely composed of two proteins FliM and FliN, whereas an analogous substructure for the closely related non-flagellar (NF) T3SS has not been observed in situ. We show that the spa33 gene encoding the putative NF-T3SS C-ring component in Shigella flexneri is alternatively translated to produce both full-length (Spa33-FL) and a short variant (Spa33-C), with both required for secretion. They associate in a 1:2 complex (Spa33-FL/C2) that further oligomerises into elongated arrays in vitro. The structure of Spa33-C2 and identification of an unexpected intramolecular pseudodimer in Spa33-FL reveal a molecular model for their higher order assembly within NF-T3SS. Spa33-FL and Spa33-C are identified as functional counterparts of a FliM-FliN fusion and free FliN respectively. Furthermore, we show that Thermotoga maritima FliM and FliN form a 1:3 complex structurally equivalent to Spa33-FL/C2 , allowing us to propose a unified model for C-ring assembly by NF-T3SS and flagellar-T3SS.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallizationCrystallography, X-RayFlagellaMass SpectrometryModels, MolecularProtein ConformationProtein MultimerizationShigella flexneriThermotoga maritimaType III Secretion SystemsBacterial ProteinsFliM protein, BacteriaFliN protein, BacteriaType III Secretion Systems

Identifiers

PMID26538516
PMCPMC4832279

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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.