ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of components of an intercellular channel complex in sporulating Bacillus subtilis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Developmentally regulated proteolysis by MdfA and ClpCP mediates metabolic differentiation duringGenes & development · 2025Article
- Deciphering metabolic differentiation during Bacillus subtilis sporulation.Nature communications · 2025Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- To Feed or to Stick? Genomic Analysis Offers Clues for the Role of a Molecular Machine in Endospore Formers.Journal of bacteriology · 2022Review
- Conservation and Evolution of the Sporulation Gene Set in Diverse Members of theJournal of bacteriology · 2022Article
- Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.Nature communications · 2021Article
- Article
- Metabolic differentiation and intercellular nurturing underpin bacterial endospore formation.Science advances · 2021Article
- Distribution and preservation of the components of the engulfment. What is beyond representative genomes?PloS one · 2021Article
- Milestones inMicrobial cell (Graz, Austria) · 2020Review
- Channels modestly impact compartment-specific ATP levels during Bacillus subtilis sporulation and a rise in the mother cell ATP level is not necessary for Pro-σMolecular microbiology · 2020Article
- The SiaABC threonine phosphorylation pathway controls biofilm formation in response to carbon availability in Pseudomonas aeruginosa.PloS one · 2020Article
- From Root to Tips: Sporulation Evolution and Specialization in Bacillus subtilis and the Intestinal Pathogen Clostridioides difficile.Molecular biology and evolution · 2019Article
- The molecular architecture of engulfment duringeLife · 2019Article
- A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective.Microbiology spectrum · 2019Review
- Peptidoglycan degradation machinery in Clostridium difficile forespore engulfment.Molecular microbiology · 2018Article
- Structural characterization of SpoIIIAB sporulation-essential protein in Bacillus subtilis.Journal of structural biology · 2018Article
- A two-step transport pathway allows the mother cell to nurture the developing spore in Bacillus subtilis.PLoS genetics · 2017Article
- Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Following asymmetric cell division during spore formation in Bacillus subtilis, a forespore expressed membrane protein SpoIIQ, interacts across an intercellular space with a mother cell-expressed membrane protein, SpoIIIAH. Their interaction can serve as a molecular "ratchet" contributing to the migration of the mother cell membrane around that of the forespore in a phagocytosis-like process termed engulfment. Upon completion of engulfment, SpoIIQ and SpoIIIAH are integral components of a recently proposed intercellular channel allowing passage from the mother cell into the forespore of factors required for late gene expression in this compartment. Here we show that the extracellular domains of SpoIIQ and SpoIIIAH form a heterodimeric complex in solution. The crystal structure of this complex reveals that SpoIIQ has a LytM-like zinc-metalloprotease fold but with an incomplete zinc coordination sphere and no metal. SpoIIIAH has an α-helical subdomain and a protruding β-sheet subdomain, which mediates interactions with SpoIIQ. SpoIIIAH has sequence and structural homology to EscJ, a type III secretion system protein that forms a 24-fold symmetric ring. Superposition of the structures of SpoIIIAH and EscJ reveals that the SpoIIIAH protomer overlaps with two adjacent protomers of EscJ, allowing us to generate a dodecameric SpoIIIAH ring by using structural homology. Following this superposition, the SpoIIQ chains also form a closed dodecameric ring abutting the SpoIIIAH ring, producing an assembly surrounding a 60 Å channel. The dimensions and organization of the proposed complex suggest it is a plausible model for the extracellular component of a gap junction-like intercellular channel.
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