Evidence map›Paper›PMID 27681621›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis.

Christopher D A Rodrigues, Xavier Henry, Emmanuelle Neumann, Vilius Kurauskas, Laure Bellard, Yann Fichou, Paul Schanda, Guy Schoehn, David Z Rudner, Cecile Morlot

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  10. Milestones inMicrobial cell (Graz, Austria) · 2020
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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

10 authors at 5 institutions in 3 countries.

Christopher D A RodriguesDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston MA 02115.
Xavier HenryInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
Emmanuelle NeumannInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
Vilius KurauskasInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
Laure BellardInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
Yann FichouInstitute for Physical Chemistry II, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Paul SchandaInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
Guy SchoehnInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France.
David Z RudnerDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston MA 02115; cecile.morlot@ibs.fr rudner@hms.harvard.edu.
Cecile MorlotInstitut de Biologie Structurale (IBS), Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, 38044 Grenoble, France; cecile.morlot@ibs.fr rudner@hms.harvard.edu.
Centre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRHarvard University · USInstitut de Biologie Structurale · FRRuhr University Bochum · DE

Funding

Chromosome Dynamics in Bacillus SubtillsR01GM086466 · NIGMS · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2009 to 2021
$4.2M
NIGMS NIH HHS R01 GM086466
6 · The paper itself

Abstract

During spore formation in Bacillus subtilis a transenvelope complex is assembled across the double membrane that separates the mother cell and forespore. This complex (called the "A-Q complex") is required to maintain forespore development and is composed of proteins with remote homology to components of type II, III, and IV secretion systems found in Gram-negative bacteria. Here, we show that one of these proteins, SpoIIIAG, which has remote homology to ring-forming proteins found in type III secretion systems, assembles into an oligomeric ring in the periplasmic-like space between the two membranes. Three-dimensional reconstruction of images generated by cryo-electron microscopy indicates that the SpoIIIAG ring has a cup-and-saucer architecture with a 6-nm central pore. Structural modeling of SpoIIIAG generated a 24-member ring with dimensions similar to those of the EM-derived saucer. Point mutations in the predicted oligomeric interface disrupted ring formation in vitro and impaired forespore gene expression and efficient spore formation in vivo. Taken together, our data provide strong support for the model in which the A-Q transenvelope complex contains a conduit that connects the mother cell and forespore. We propose that a set of stacked rings spans the intermembrane space, as has been found for type III secretion systems.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsComputer SimulationCryoelectron MicroscopyImaging, Three-DimensionalMagnetic Resonance SpectroscopyModels, MolecularMutationOperonProtein DomainsSequence Homology, Amino AcidSpores, BacterialBacterial ProteinsEscJ/PrgK/FliFSigGSpoIIIAGsporulationtype III secretion system

Identifiers

PMID27681621
PMCPMC5068255
OpenAlexW2527153616

What OpenQuestion holds

Textmetadata
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.