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Biomolecular condensate drives polymerization and bundling of the bacterial tubulin FtsZ to regulate cell division

Author

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  • Beatrice Ramm

    (Max Planck Institute of Biochemistry
    Princeton University)

  • Dominik Schumacher

    (Max Planck Institute for Terrestrial Microbiology)

  • Andrea Harms

    (Max Planck Institute for Terrestrial Microbiology)

  • Tamara Heermann

    (Max Planck Institute of Biochemistry)

  • Philipp Klos

    (Max Planck Institute for Terrestrial Microbiology)

  • Franziska Müller

    (Max Planck Institute for Terrestrial Microbiology)

  • Petra Schwille

    (Max Planck Institute of Biochemistry)

  • Lotte Søgaard-Andersen

    (Max Planck Institute for Terrestrial Microbiology)

Abstract

Cell division is spatiotemporally precisely regulated, but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the PomX/PomY/PomZ proteins form a single megadalton-sized complex that directly positions and stimulates cytokinetic ring formation by the tubulin homolog FtsZ. Here, we study the structure and mechanism of this complex in vitro and in vivo. We demonstrate that PomY forms liquid-like biomolecular condensates by phase separation, while PomX self-assembles into filaments generating a single large cellular structure. The PomX structure enriches PomY, thereby guaranteeing the formation of precisely one PomY condensate per cell through surface-assisted condensation. In vitro, PomY condensates selectively enrich FtsZ and nucleate GTP-dependent FtsZ polymerization and bundle FtsZ filaments, suggesting a cell division site positioning mechanism in which the single PomY condensate enriches FtsZ to guide FtsZ-ring formation and division. This mechanism shares features with microtubule nucleation by biomolecular condensates in eukaryotes, supporting this mechanism’s ancient origin.

Suggested Citation

  • Beatrice Ramm & Dominik Schumacher & Andrea Harms & Tamara Heermann & Philipp Klos & Franziska Müller & Petra Schwille & Lotte Søgaard-Andersen, 2023. "Biomolecular condensate drives polymerization and bundling of the bacterial tubulin FtsZ to regulate cell division," Nature Communications, Nature, vol. 14(1), pages 1-24, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39513-2
    DOI: 10.1038/s41467-023-39513-2
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    References listed on IDEAS

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    3. Matthew R. King & Sabine Petry, 2020. "Phase separation of TPX2 enhances and spatially coordinates microtubule nucleation," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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    Cited by:

    1. María Pérez-Burgos & Marco Herfurth & Andreas Kaczmarczyk & Andrea Harms & Katrin Huber & Urs Jenal & Timo Glatter & Lotte Søgaard-Andersen, 2024. "A deterministic, c-di-GMP-dependent program ensures the generation of phenotypically similar, symmetric daughter cells during cytokinesis," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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