ArticleNature communications2024
Ultrastructure of macromolecular assemblies contributing to bacterial spore resistance revealed by in situ cryo-electron tomography.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Reliable delineation ofMicrobiology spectrum · 2026Article
- Real-time nanoscale investigation of spore coat assembly in Bacillus subtilis.Communications biology · 2025Article
- Optimizing MALDI-TOF Mass Spectrometry for the Identification ofInternational journal of molecular sciences · 2025Article
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- How to build the virtual cell with artificial intelligence: Priorities and opportunities.Cell · 2024Article
- How to Build the Virtual Cell with Artificial Intelligence: Priorities and Opportunities.ArXiv · 2024Article
- Cryo-electron tomography of stationary phasemicroPublication biology · 2024Article
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
Abstract
Bacterial spores owe their incredible resistance capacities to molecular structures that protect the cell content from external aggressions. Among the determinants of resistance are the quaternary structure of the chromosome and an extracellular shell made of proteinaceous layers (the coat), the assembly of which remains poorly understood. Here, in situ cryo-electron tomography on lamellae generated by cryo-focused ion beam micromachining provides insights into the ultrastructural organization of Bacillus subtilis sporangia. The reconstructed tomograms reveal that early during sporulation, the chromosome in the forespore adopts a toroidal structure harboring 5.5-nm thick fibers. At the same stage, coat proteins at the surface of the forespore form a stack of amorphous or structured layers with distinct electron density, dimensions and organization. By analyzing mutant strains using cryo-electron tomography and transmission electron microscopy on resin sections, we distinguish seven nascent coat regions with different molecular properties, and propose a model for the contribution of coat morphogenetic proteins.
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