ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the basal components of a bacterial transporter.
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 36 papers.
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.
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.
Who cites it
36 citing papers in PubMed, 60 citations in OpenAlex.
- Continuous exchange of an inner-membrane ring component is required for assembly and function of the type III secretion system.Nature communications · 2025Article
- Developmentally regulated proteolysis by MdfA and ClpCP mediates metabolic differentiation duringGenes & development · 2025Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- GroEL Secreted fromMicroorganisms · 2023Article
- Article
- 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
- 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
- Shaping an Endospore: Architectural Transformations DuringAnnual review of microbiology · 2020Review
- 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
- GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.Molecular microbiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteins SpoIIQ and SpoIIIAH interact through two membranes to connect the forespore and the mother cell during endospore development in the bacterium Bacillus subtilis. SpoIIIAH consists of a transmembrane segment and an extracellular domain with similarity to YscJ proteins. YscJ proteins form large multimeric rings that are the structural scaffolds for the assembly of type III secretion systems in gram-negative bacteria. The predicted ring-forming motif of SpoIIIAH and other evidence led to the model that SpoIIQ and SpoIIIAH form the core components of a channel or transporter through which the mother cell nurtures forespore development. Therefore, to understand the roles of SpoIIIAH and SpoIIQ in channel formation, it is critical to determine whether SpoIIIAH adopts a ring-forming structural motif, and whether interaction of SpoIIIAH with SpoIIQ would preclude ring formation. We report a 2.8-Å resolution structure of a complex of SpoIIQ and SpoIIIAH. SpoIIIAH folds into the ring-building structural motif, and modeling shows that the structure of the SpoIIQ-SpoIIIAH complex is compatible with forming a symmetrical oligomer that is similar to those in type III systems. The inner diameters of the two most likely ring models are large enough to accommodate several copies of other integral membrane proteins. SpoIIQ contains a LytM domain, which is found in metalloendopeptidases, but lacks residues important for metalloprotease activity. Other LytM domains appear to be involved in protein-protein interactions. We found that the LytM domain of SpoIIQ contains an accessory region that interacts with SpoIIIAH.
Indexed as
Identifiers
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.