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Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM

Author

Listed:
  • Yijia Cheng

    (Shanghai Jiao Tong University)

  • Mark A. B. Kreutzberger

    (University of Virginia School of Medicine)

  • Jianting Han

    (Shanghai Jiao Tong University)

  • Edward H. Egelman

    (University of Virginia School of Medicine)

  • Qin Cao

    (Shanghai Jiao Tong University)

Abstract

Protein filaments are ubiquitous in nature and have diverse biological functions. Cryo-electron microscopy (cryo-EM) enables the determination of atomic structures, even from native samples, and is capable of identifying previously unknown filament species through high-resolution cryo-EM maps. In this study, we determine the structure of an unreported filament species from a cryo-EM dataset collected from Bacillus amyloiquefaciens biofilms. These filaments are composed of GerQ, a spore coat protein known to be involved in Bacillus spore germination. GerQ assembles into a structurally stable architecture consisting of rings containing nine subunits, which stacks to form filaments. Molecular dockings and model predictions suggest that this nine-subunit structure is suitable for binding CwlJ, a protein recruited by GerQ and essential for Ca2+-DPA induced spore germination. While the assembly state of GerQ within the spores and the direct interaction between GerQ and CwlJ have yet to be validated through further experiments, our findings provide valuable insights into the self-assembly of GerQ and enhance our understanding of its role in spore germination.

Suggested Citation

  • Yijia Cheng & Mark A. B. Kreutzberger & Jianting Han & Edward H. Egelman & Qin Cao, 2024. "Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-52422-2
    DOI: 10.1038/s41467-024-52422-2
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    References listed on IDEAS

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    1. Josh Abramson & Jonas Adler & Jack Dunger & Richard Evans & Tim Green & Alexander Pritzel & Olaf Ronneberger & Lindsay Willmore & Andrew J. Ballard & Joshua Bambrick & Sebastian W. Bodenstein & David , 2024. "Accurate structure prediction of biomolecular interactions with AlphaFold 3," Nature, Nature, vol. 630(8016), pages 493-500, June.
    2. Yijia Cheng & Jianting Han & Meinai Song & Shuqin Zhang & Qin Cao, 2023. "Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    3. Yi Xiao Jiang & Qin Cao & Michael R. Sawaya & Romany Abskharon & Peng Ge & Michael DeTure & Dennis W. Dickson & Janine Y. Fu & Rachel R. Ogorzalek Loo & Joseph A. Loo & David S. Eisenberg, 2022. "Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43," Nature, Nature, vol. 605(7909), pages 304-309, May.
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