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  A phase-separated biomolecular condensate nucleates polymerization of the tubulin homolog FtsZ to spatiotemporally regulate bacterial cell division

Ramm, B., Schumacher, D., Harms, A., Heermann, T., Klos, P., Müller, F., et al. (2022). A phase-separated biomolecular condensate nucleates polymerization of the tubulin homolog FtsZ to spatiotemporally regulate bacterial cell division. bioRxiv: the preprint server for biology, 2022.09.12.507586.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-06FC-3 Version Permalink: https://hdl.handle.net/21.11116/0000-000F-6914-5
Genre: Preprint

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Locator:
https://doi.org/10.1101/2022.09.12.507586 (Preprint)
Description:
Preprint
OA-Status:
Green
Locator:
http://dx.doi.org/10.1038/s41467-023-39513-2 (Publisher version)
Description:
Verlagsversion
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, predatory bacterium Myxococcus xanthus, the PomX/PomY/PomZ proteins form a single large megadalton-sized complex that directly positions and stimulates cytokinetic ring formation by the tubulin homolog FtsZ. Here, we studied 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, suggesting a novel cell division site positioning mechanism in which the single PomY condensate enriches FtsZ to guide FtsZ-ring formation and division. PomY-nucleated FtsZ polymerization shares features with microtubule nucleation by biomolecular condensates in eukaryotes, supporting this mechanism's ancient origin.Competing Interest StatementThe authors have declared no competing interest.

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Language(s): eng - English
 Dates: 2022-09-12
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: No review
 Identifiers: DOI: 10.1101/2022.09.12.507586
bioRxiv: 2022.09.12.507586
 Degree: -

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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 : in part
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)
Project name : -
Grant ID : -
Funding program : -
Funding organization : Max Planck Society
Project name : -
Grant ID : -
Funding program : a joint funding initiative of the German Federal Ministry of 613 Education and Research (BMBF)
Funding organization : research network MaxSynBio

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Title: bioRxiv : the preprint server for biology
  Abbreviation : bioRxiv
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: 2022.09.12.507586 Start / End Page: - Identifier: ZDB: 2766415-6
CoNE: https://pure.mpg.de/cone/journals/resource/2766415-6