ArticleEMBO reports2019
Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA.
Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 2026Article
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- Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026Article
- Glycerol-Driven Energy and Proteostasis Underpin Antibiotic Tolerance inbioRxiv : the preprint server for biology · 2026Article
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- Identifying Subcellular Structure Components in Escherichia Coli by Crosslinking and SEC-MS.Proteomics · 2026Article
- Mechano-induced patterned domain formation by monocytes.Nature materials · 2026Article
- The chromosomal origin of replication as the basis for the spatio-temporal biology of bacteria.Frontiers in microbiology · 2026Review
- Benzodioxane-benzamides targeting bacterial cell division protein FtsZ potentially disrupt SlmA-mediated nucleoid occlusion and reversible biomolecular condensation.International journal of biological macromolecules · 2025Article
- Trimerization domain-interfering peptide inhibits EML4-ALK condensate formation, fusion-dependent signaling, and cell growth.Molecular biology of the cell · 2025Article
- Mechanisms and Pathological Significance of Liquid-Liquid Phase Separation in Bacteria.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Controlling Multiphase Coacervate Wetting and Self-Organization by Interfacial Proteins.Journal of the American Chemical Society · 2025Article
- Evidence for biomolecular condensates formed by the Escherichia coli MatP protein in spatiotemporal regulation of the bacterial cell division cycle.International journal of biological macromolecules · 2025Article
- How do spherical bacteria regulate cell division?Biochemical Society transactions · 2025Review
- 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
- Interplay between membranes and biomolecular condensates in the regulation of membrane-associated cellular processes.Experimental & molecular medicine · 2024Review
- RNA-driven phase transitions in biomolecular condensates.Molecular cell · 2024Review
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- Dynamic structure of E. coli cytoplasm: supramolecular complexes and cell aging impact spatial distribution and mobility of proteins.Communications biology · 2024Article
- Maturation and Conformational Switching of aJournal of the American Chemical Society · 2024Article
11 more citing papers are in PubMed but not listed here.
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8 authors.
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Abstract
Macromolecular condensation resulting from biologically regulated liquid-liquid phase separation is emerging as a mechanism to organize intracellular space in eukaryotes, with broad implications for cell physiology and pathology. Despite their small size, bacterial cells are also organized by proteins such as FtsZ, a tubulin homolog that assembles into a ring structure precisely at the cell midpoint and is required for cytokinesis. Here, we demonstrate that FtsZ can form crowding-induced condensates, reminiscent of those observed for eukaryotic proteins. Formation of these FtsZ-rich droplets occurs when FtsZ is bound to SlmA, a spatial regulator of FtsZ that antagonizes polymerization, while also binding to specific sites on chromosomal DNA. The resulting condensates are dynamic, allowing FtsZ to undergo GTP-driven assembly to form protein fibers. They are sensitive to compartmentalization and to the presence of a membrane boundary in cell mimetic systems. This is a novel example of a bacterial nucleoprotein complex exhibiting condensation into liquid droplets, suggesting that phase separation may also play a functional role in the spatiotemporal organization of essential bacterial processes.
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