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| Title | In situ architecture of a nucleoid-associated biomolecular co-condensate that regulates bacterial cell division. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 122, Issue 1, Page e2419610121, Year 2025 |
| Publish date | Jan 7, 2025 |
 Authors | Peng Xu / Dominik Schumacher / Chuan Liu / Andrea Harms / Marcel Dickmanns / Florian Beck / Jürgen M Plitzko / Wolfgang Baumeister / Lotte Søgaard-Andersen /  |
| PubMed Abstract | In most bacteria, cell division depends on the tubulin-homolog FtsZ that polymerizes in a GTP-dependent manner to form the cytokinetic Z-ring at the future division site. Subsequently, the Z-ring ...In most bacteria, cell division depends on the tubulin-homolog FtsZ that polymerizes in a GTP-dependent manner to form the cytokinetic Z-ring at the future division site. Subsequently, the Z-ring recruits, directly or indirectly, all other proteins of the divisome complex that executes cytokinesis. A critical step in this process is the precise positioning of the Z-ring at the future division site. While the divisome proteins are generally conserved, the regulatory systems that position the Z-ring are more diverse. However, these systems have in common that they modulate FtsZ polymerization. In PomX, PomY, and PomZ form precisely one MDa-sized, nonstoichiometric, nucleoid-associated assembly that spatiotemporally guides Z-ring formation. Here, using cryo-correlative light and electron microscopy together with in situ cryoelectron tomography, we determine the PomXYZ assembly's architecture at close-to-live conditions. PomX forms a porous meshwork of randomly intertwined filaments. Templated by this meshwork, the phase-separating PomY protein forms a biomolecular condensate that compacts and bends the PomX filaments, resulting in the formation of a selective PomXYZ co-condensate that is associated to the nucleoid by PomZ. These studies reveal a hitherto undescribed supramolecular structure and provide a framework for understanding how a nonstoichiometric co-condensate forms, maintains number control, and nucleates GTP-dependent FtsZ polymerization to precisely regulate cell division. |
 External links | Proc Natl Acad Sci U S A / PubMed:39739804 / PubMed Central |
| Methods | EM (subtomogram averaging) / EM (single particle) |
| Resolution | 6.0 - 10.0 Å |
| Structure data |  EMDB-50504: in situ 70S Myxococcus xanthus ribosome  EMDB-50515: PomX filament from Myxococcus xanthus |
| Source |
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Myxococcus xanthus (bacteria)