ArticleNature communications2023
Biomolecular condensate drives polymerization and bundling of the bacterial tubulin FtsZ to regulate cell division.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 34 citations in OpenAlex.
- A New Anatomy of Autophagic Clearance: On the Roles of Intrinsic Disorder in the Membrane-Less on Membrane-Encapsulated Mechanism.Membranes · 2026Review
- Capillary bundling of microtubules by condensates.bioRxiv : the preprint server for biology · 2026Article
- Bacterial L-forms: Key Mechanisms of Drug Resistance, Disease Recurrence, and Immune Evasion.Indian journal of microbiology · 2026Review
- Bottom-Up Coacervate-Based Artificial Cells: Integrating Cellular Hallmarks into Complex Life-Like Systems.Angewandte Chemie (International ed. in English) · 2026Review
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- Phase separation induced by active polymerization makes protocells robust against environmental changes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The chromosomal origin of replication as the basis for the spatio-temporal biology of bacteria.Frontiers in microbiology · 2026Review
- Automated navigation of condensate phase behavior with active machine learning.Nature communications · 2025Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- A blueprint for biomolecular condensation driven by bacterial microcompartment encapsulation peptides.Nature communications · 2025Article
- Milestones in the development ofJournal of bacteriology · 2025Review
- Phase Separation: Orchestrating Biological Adaptations to Environmental Fluctuations.International journal of molecular sciences · 2025Review
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- In situ architecture of a nucleoid-associated biomolecular co-condensate that regulates bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- DNA Sensor ABCF1 Phase Separates With cccDNA to Inhibit Hepatitis B Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Hypothesis: bacteria live on the edge of phase transitions with a cell cycle regulated by a water-clock.Theory in biosciences = Theorie in den Biowissenschaften · 2024Article
- Frequent and asymmetric cell division in endosymbiotic bacteria of cockroaches.Applied and environmental microbiology · 2024Article
- Memory effects of transcription regulator-DNA interactions in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Supramolecular fibrillation in coacervates and other confined systems towards biomimetic function.Communications chemistry · 2024Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.