ArticlePloS one2010
In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM).
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.
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Who cites it
144 citing papers in PubMed, 275 citations in OpenAlex.
- Article
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Light-dependent modulation of protein localization and function in living bacteria cells.Nature communications · 2024Article
- Stay on track - revelations of bacterial cell wall synthesis enzymes and things that go by single-molecule imaging.Current opinion in microbiology · 2024Review
- Protocol for single-molecule labeling and tracking of bacterial cell division proteins.STAR protocols · 2024Article
- N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure.Frontiers in microbiology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Application of nanotags and nanobodies for live cell single-molecule imaging of the Z-ring in Escherichia coli.Current genetics · 2023Article
- Arginine methylation sites on SepIVA help balance elongation and septation in Mycobacterium smegmatis.Molecular microbiology · 2023Article
- Chiral and nematic phases of flexible active filaments.Nature physics · 2023Article
- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.Nature communications · 2022Article
- Assembly dynamics of FtsZ and DamX during infection-related filamentation and division in uropathogenic E. coli.Nature communications · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- A pairwise distance distribution correction (DDC) algorithm to eliminate blinking-caused artifacts in SMLM.Nature methods · 2021Article
- Measurement of Protein Mobility inFrontiers in microbiology · 2021Article
- Single-molecule localization microscopy.Nature reviews. Methods primers · 2021Article
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
- Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.Annual review of biophysics · 2020Review
84 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The FtsZ protein, a tubulin-like GTPase, plays a pivotal role in prokaryotic cell division. In vivo it localizes to the midcell and assembles into a ring-like structure-the Z-ring. The Z-ring serves as an essential scaffold to recruit all other division proteins and generates contractile force for cytokinesis, but its supramolecular structure remains unknown. Electron microscopy (EM) has been unsuccessful in detecting the Z-ring due to the dense cytoplasm of bacterial cells, and conventional fluorescence light microscopy (FLM) has only provided images with limited spatial resolution (200-300 nm) due to the diffraction of light. Hence, given the small sizes of bacteria cells, identifying the in vivo structure of the Z-ring presents a substantial challenge. Here, we used photoactivated localization microscopy (PALM), a single molecule-based super-resolution imaging technique, to characterize the in vivo structure of the Z-ring in E. coli. We achieved a spatial resolution of ∼35 nm and discovered that in addition to the expected ring-like conformation, the Z-ring of E. coli adopts a novel compressed helical conformation with variable helical length and pitch. We measured the thickness of the Z-ring to be ∼110 nm and the packing density of FtsZ molecules inside the Z-ring to be greater than what is expected for a single-layered flat ribbon configuration. Our results strongly suggest that the Z-ring is composed of a loose bundle of FtsZ protofilaments that randomly overlap with each other in both longitudinal and radial directions of the cell. Our results provide significant insight into the spatial organization of the Z-ring and open the door for further investigations of structure-function relationships and cell cycle-dependent regulation of the Z-ring.
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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.