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

Beatrice Ramm (), Dominik Schumacher (), Andrea Harms, Tamara Heermann, Philipp Klos, Franziska Müller, Petra Schwille () and Lotte Søgaard-Andersen ()
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Beatrice Ramm: Max Planck Institute of Biochemistry
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

Nature Communications, 2023, vol. 14, issue 1, 1-24

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-39513-2

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