ArticleJournal of bacteriology2012
Physical interaction between coat morphogenetic proteins SpoVID and CotE is necessary for spore encasement in Bacillus subtilis.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- The calcium signal regulatory network and the roles of calcium-binding proteins in bacteria.World journal of microbiology & biotechnology · 2026Review
- Identification of SpoVID as a putative new substrate of the sporulation-specific protease YabG inFrontiers in microbiology · 2026Article
- To Sporulate or Not to Sporulate: Developmental Checkpoints MonitoringAnnual review of microbiology · 2025Review
- Disruption of Spore Coat Integrity inCurrent issues in molecular biology · 2025Article
- Article
- Embedding a ribonuclease in the spore crust couples gene expression to spore development in Bacillus subtilis.Nucleic acids research · 2025Article
- Ultrastructure of macromolecular assemblies contributing to bacterial spore resistance revealed by in situ cryo-electron tomography.Nature communications · 2024Article
- Review
- Conservation and Evolution of the Sporulation Gene Set in Diverse Members of theJournal of bacteriology · 2022Article
- Bacterial developmental checkpoint that directly monitors cell surface morphogenesis.Developmental cell · 2022Article
- The Morphogenetic Protein CotE Positions Exosporium Proteins CotY and ExsY during Sporulation of Bacillus cereus.mSphere · 2021Article
- Interactions ofMicroorganisms · 2021Article
- A dynamic, ring-forming MucB / RseB-like protein influences spore shape in Bacillus subtilis.PLoS genetics · 2020Article
- From Root to Tips: Sporulation Evolution and Specialization in Bacillus subtilis and the Intestinal Pathogen Clostridioides difficile.Molecular biology and evolution · 2019Article
- Sporulation and Germination in Clostridial Pathogens.Microbiology spectrum · 2019Review
- A LysM Domain Intervenes in Sequential Protein-Protein and Protein-Peptidoglycan Interactions Important for Spore Coat Assembly inJournal of bacteriology · 2019Article
- SpoVID functions as a non-competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis.Molecular microbiology · 2018Article
- Stoichiometry, Absolute Abundance, and Localization of Proteins in the Bacillus cereus Spore Coat Insoluble Fraction Determined Using a QconCAT Approach.Journal of proteome research · 2018Article
- CotG-Like Modular Proteins Are Common among Spore-Forming Bacilli.Journal of bacteriology · 2016Article
- Ellipsoid Localization Microscopy Infers the Size and Order of Protein Layers in Bacillus Spore Coats.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Endospore formation by Bacillus subtilis is a complex and dynamic process. One of the major challenges of sporulation is the assembly of a protective, multilayered, proteinaceous spore coat, composed of at least 70 different proteins. Spore coat formation can be divided into two distinct stages. The first is the recruitment of proteins to the spore surface, dependent on the morphogenetic protein SpoIVA. The second step, known as encasement, involves the migration of the coat proteins around the circumference of the spore in successive waves, a process dependent on the morphogenetic protein SpoVID and the transcriptional regulation of individual coat genes. We provide genetic and biochemical evidence supporting the hypothesis that SpoVID promotes encasement of the spore by establishing direct protein-protein interactions with other coat morphogenetic proteins. It was previously demonstrated that SpoVID directly interacts with SpoIVA and the inner coat morphogenetic protein, SafA. Here, we show by yeast two-hybrid and pulldown assays that SpoVID also interacts directly with the outer coat morphogenetic protein, CotE. Furthermore, by mutational analysis, we identified a specific residue in the N-terminal domain of SpoVID that is essential for the interaction with CotE but dispensable for the interaction with SafA. We propose an updated model of coat assembly and spore encasement that incorporates several physical interactions between the principal coat morphogenetic proteins.
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Registered trials
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.