ArticleBiophysical journal2012
Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- Cold Atmospheric-Pressure Plasma Caused Protein Damage in Methicillin-ResistantMicroorganisms · 2021Article
- FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.Antibiotics (Basel, Switzerland) · 2021Review
- Surface Orientation and Binding Strength Modulate Shape of FtsZ on Lipid Surfaces.International journal of molecular sciences · 2019Article
- Gain-of-function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling.Molecular microbiology · 2018Article
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- Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Biophysical journal · 2017Article
- ZipA and FtsA* stabilize FtsZ-GDP miniring structures.Scientific reports · 2017Article
- The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red AlgaThe Journal of biological chemistry · 2017Article
- Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.Journal of bacteriology · 2017Article
- Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.Biopolymers · 2016Article
- Defining the rate-limiting processes of bacterial cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.The Journal of biological chemistry · 2016Article
- The bacterial divisome: ready for its close-up.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
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- Bacterial cell division: experimental and theoretical approaches to the divisome.Science progress · 2015Review
- Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division.eLife · 2014Article
- Understanding nucleotide-regulated FtsZ filament dynamics and the monomer assembly switch with large-scale atomistic simulations.Biophysical journal · 2014Article
- Multifunctional roles for the protein translocation machinery in RNA anchoring to the endoplasmic reticulum.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
FtsZ, the primary cytoskeletal element of the Z ring, which constricts to divide bacteria, assembles into short, one-stranded filaments in vitro. These must be further assembled to make the Z ring in bacteria. Conventional electron microscopy (EM) has failed to image the Z ring or resolve its substructure. Here we describe a procedure that enabled us to image reconstructed, inside-out FtsZ rings by negative-stain EM, revealing the arrangement of filaments. We took advantage of a unique lipid that spontaneously forms 500 nm diameter tubules in solution. We optimized conditions for Z-ring assembly with fluorescence light microscopy and then prepared specimens for negative-stain EM. Reconstituted FtsZ rings, encircling the tubules, were clearly resolved. The rings appeared as ribbons of filaments packed side by side with virtually no space between neighboring filaments. The rings were separated by variable expanses of empty tubule as seen by light microscopy or EM. The width varied considerably from one ring to another, but each ring maintained a constant width around its circumference. The inside-out FtsZ rings moved back and forth along the tubules and exchanged subunits with solution, similarly to Z rings reconstituted outside or inside tubular liposomes. FtsZ from Escherichia coli and Mycobacterium tuberculosis assembled rings of similar structure, suggesting a universal structure across bacterial species. Previous models for the Z ring in bacteria have favored a structure of widely scattered filaments that are not in contact. The ribbon structure that we discovered here for reconstituted inside-out FtsZ rings provides what to our knowledge is new evidence that the Z ring in bacteria may involve lateral association of protofilaments.
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Registered trials
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.