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

Ramm, B., Schumacher, D., Harms, A., Heermann, T., Klos, P., Müller, F., et al. (2023). Biomolecular condensate drives polymerization and bundling of the bacterial tubulin FtsZ to regulate cell division. Nature Communications, 14(1): 3825. doi:10.1038/s41467-023-39513-2.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000D-5BF6-8 Version Permalink: https://hdl.handle.net/21.11116/0000-000F-2046-E
Genre: Journal Article

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https://doi.org/10.1038/s41467-023-39513-2 (Publisher version)
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OA-Status:
Gold

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 Creators:
Ramm, Beatrice, Author
Schumacher, Dominik1, Author           
Harms, Andrea1, Author           
Heermann, Tamara, Author
Klos, Philipp1, Author           
Müller, Franziska1, Author           
Schwille, Petra, Author
Søgaard-Andersen, Lotte1, Author                 
Affiliations:
1Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266305              

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 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.

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Language(s): eng - English
 Dates: 2023-06-28
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: URI: https://doi.org/10.1038/s41467-023-39513-2
DOI: 10.1038/s41467-023-39513-2
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Project name : Fellowship
Grant ID : -
Funding program : Graduate School of Quantitative Biosciences Munich
Funding organization : German Research Council (DFG)
Project name : -
Grant ID : PHY-1734030
Funding program : -
Funding organization : National Science Foundation
Project name : -
Grant ID : 269423233
Funding program : Transregio 174 “Spatiotemporal dynamics of bacterial cells”
Funding organization : German Research Council (DFG)
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Grant ID : -
Funding program : -
Funding organization : Max Planck Society
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Grant ID : -
Funding program : a joint funding initiative of the German Federal Ministry of Education and Research (BMBF)
Funding organization : esearch network MaxSynBio
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Grant ID : -
Funding program : Open Access
Funding organization : Projekt DEAL

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
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Publ. Info: London : Nature Publishing Group
Pages: 3825 Volume / Issue: 14 (1) Sequence Number: 3825 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723