ArticleThe EMBO journal2004
Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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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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.
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Who cites it
30 citing papers in PubMed, 59 citations in OpenAlex.
- SpoIIIL is a forespore factor required for efficient cell-cell signalling during Bacillus subtilis sporulation.PLoS genetics · 2025Article
- Ribosomes translocation into the spore of Bacillus subtilis is highly organised and requires peptidoglycan rearrangements.Nature communications · 2025Article
- Article
- Shaping an Endospore: Architectural Transformations DuringAnnual review of microbiology · 2020Review
- Article
- Microdomain formation is a general property of bacterial membrane proteins and induces heterogeneity of diffusion patterns.BMC biology · 2018Article
- GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.Molecular microbiology · 2016Article
- Localization of a red fluorescence protein adsorbed on wild type and mutant spores of Bacillus subtilis.Microbial cell factories · 2016Article
- The SpoIIQ-SpoIIIAH complex of Clostridium difficile controls forespore engulfment and late stages of gene expression and spore morphogenesis.Molecular microbiology · 2016Article
- Regulation of Clostridium difficile Spore Formation by the SpoIIQ and SpoIIIA Proteins.PLoS genetics · 2015Article
- The SpoIIQ landmark protein has different requirements for septal localization and immobilization.Molecular microbiology · 2013Article
- Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis.Molecular microbiology · 2013Article
- Stably bridging a great divide: localization of the SpoIIQ landmark protein in Bacillus subtilis.Molecular microbiology · 2013Article
- Global analysis of the sporulation pathway of Clostridium difficile.PLoS genetics · 2013Article
- Structure of components of an intercellular channel complex in sporulating Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Recent progress in Bacillus subtilis sporulation.FEMS microbiology reviews · 2012Review
- Loss of compartmentalization of σ(E) activity need not prevent formation of spores by Bacillus subtilis.Journal of bacteriology · 2010Article
- Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation.Journal of molecular biology · 2010Article
- Novel secretion apparatus maintains spore integrity and developmental gene expression in Bacillus subtilis.PLoS genetics · 2009Article
- Processing of a membrane protein required for cell-to-cell signaling during endospore formation in Bacillus subtilis.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In Bacillus subtilis, many membrane proteins localize to the sporulation septum, where they play key roles in spore morphogenesis and cell-specific gene expression, but the mechanism for septal targeting is not well understood. SpoIIQ, a forespore-expressed protein, is involved in engulfment and forespore-specific gene expression. We find that SpoIIQ dynamically localizes to the sporulation septum, tracks the engulfing mother cell membrane, assembles into helical arcs around the forespore and is finally degraded. Retention of SpoIIQ in the septum requires one or more mother cell-expressed proteins. We also observed that any forespore-expressed membrane protein initially localizes to the septum and later spreads throughout the forespore membrane, suggesting that membrane protein insertion occurs at the forespore septal region. This possibility provides an attractive mechanism for how activation of mother cell-specific gene expression is restricted to adjacent sister cells, since direct insertion of the signaling protein SpoIIR into the septum would spatially restrict its activity. In keeping with this hypothesis, we find that SpoIIR localizes to the septum and is transiently expressed.
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What OpenQuestion holds
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.