Evidence map›Paper›PMID 24810258›Full record

ArticleFEMS microbiology letters2014

An autoinhibitory conformation of the Bacillus subtilis spore coat protein SpoIVA prevents its premature ATP-independent aggregation.

Jean-Philippe Castaing, Scarlett Lee, Vivek Anantharaman, Geoffrey E Ravilious, L Aravind, Kumaran S Ramamurthi

Open access · bronzeAbstract readLetter
In one paragraph

Article in FEMS microbiology letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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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  8. Article
  9. Article
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  11. Article
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  15. A 2-dimensional ratchet model describes assembly initiation of a specialized bacterial cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. Review
  18. Article
  19. Structural basis for the geometry-driven localization of a small protein.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. 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

6 authors at 3 institutions in 2 countries.

Jean-Philippe CastaingLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Scarlett Lee
Vivek Anantharaman
Geoffrey E Ravilious
L Aravind
Kumaran S Ramamurthi
MRC Laboratory of Molecular Biology · GBNational Institutes of Health · USNational Institute of Allergy and Infectious Diseases · US

Funding

Subcellular protein localization in B. subtilisZIABC011211 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RAMAMURTHI, KUMARAN · 2009 to 2025
$21.4M
Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC011211
6 · The paper itself

Abstract

Spores of Bacillus subtilis are dormant cell types that are formed when the bacterium encounters starvation conditions. Spores are encased in a shell, termed the coat, which is composed of approximately seventy different proteins and protects the spore's genetic material from environmental insults. The structural component of the basement layer of the coat is an exceptional cytoskeletal protein, termed SpoIVA, which binds and hydrolyzes ATP. ATP hydrolysis is utilized to drive a conformational change in SpoIVA that leads to its irreversible self-assembly into a static polymer in vitro. Here, we characterize the middle domain of SpoIVA, the predicted secondary structure of which resembles the chemotaxis protein CheX but, unlike CheX, does not harbor residues required for phosphatase activity. Disruptions in this domain did not abolish ATP hydrolysis, but resulted in mislocalization of the protein and reduction in sporulation efficiency in vivo. In vitro, disruptions in this domain prevented the ATP hydrolysis-driven conformational change in SpoIVA required for polymerization and led to the aggregation of SpoIVA into particles that did not form filaments. We propose a model in which SpoIVA initially assumes a conformation in which it inhibits its own aggregation into particles, and that ATP hydrolysis remodels the protein so that it assumes a polymerization-competent conformation.

Indexed as

Protein MultimerizationAdenosine TriphosphateAmino Acid SequenceBacillus subtilisBacterial ProteinsDNA Mutational AnalysisHydrolysisModels, MolecularMolecular Sequence DataProtein ConformationSequence AlignmentSpores, BacterialAdenosine TriphosphateBacterial Proteinsspore-specific proteins, BacillusactincortexlocalizationsporulationSpoVMtubulin

Identifiers

PMID24810258
PMCPMC4172660
OpenAlexW2064985052

What OpenQuestion holds

Textmetadata
LicenceTDM
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.