Evidence map›Paper›PMID 30168214›Full record

ArticleMolecular microbiology2018

SpoVID functions as a non-competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis.

Filipa Nunes, Catarina Fernandes, Carolina Freitas, Eleonora Marini, Mónica Serrano, Charles P Moran, Patrick Eichenberger, Adriano O Henriques

Abstract read
In one paragraph

Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  6. Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

8 authors.

Filipa NunesMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Catarina FernandesMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Carolina FreitasMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Eleonora MariniMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Mónica SerranoMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Charles P MoranDepartment of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Patrick EichenbergerDepartment of Biology, New York University, New York, NY, 10003, USA.
Adriano O HenriquesMicrobial Development Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.

Funding

A systems level analysis of spore coat assembly in Bacillus subtilisR01GM081571 · NIGMS · NEW YORK UNIVERSITY · PI EICHENBERGER, PATRICK · 2008 to 2012
$1.5M
An Intercellular Connection in Endospore DevelopmentR01GM110000 · NIGMS · EMORY UNIVERSITY · PI MORAN, CHARLES P. · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM081571NIGMS NIH HHS R01 GM110000
6 · The paper itself

Abstract

During sporulation in Bacillus subtilis, a group of mother cell-specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coat layers. Targeting of coat proteins to the developing spore is followed by encasement. Encasement by SafA and CotE requires E, a region of 11 amino acids in the encasement protein SpoVID, with which CotE interacts directly. Here, we identified two single alanine substitutions in E that prevent binding of SafA, but not of CotE, to SpoVID, and block encasement. The substitutions result in the accumulation of SafA, CotE and their dependent proteins at the mother cell proximal spore pole, phenocopying a spoVID null mutant and suggesting that mislocalized SafA acts as an attractor for the rest of the coat. The requirement for E in SafA binding is bypassed by a peptide with the sequence of E provided in trans. We suggest that E allows binding of SafA to a second region in SpoVID, enabling CotE to interact with E and SpoVID to function as a non-competitive hub during spore encasement.

Indexed as

Amino Acid SubstitutionBacillus subtilisBacterial ProteinsMembrane ProteinsProtein DomainsSpores, BacterialBacterial ProteinsCotE protein, Bacillus subtilisMembrane ProteinsSafA protein, Bacillus subtilisspoVID protein, Bacillus subtilis

Identifiers

PMID30168214
PMCPMC6282716

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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.