ArticleProceedings of the National Academy of Sciences of the United States of America2018
FtsZ filaments have the opposite kinetic polarity of microtubules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- A Division-Associated Envelope Protein, MAB_2363, Drives Intrinsic Resistance and Virulence inMicroorganisms · 2026Article
- Article
- Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota.The EMBO journal · 2025Article
- A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.Nature communications · 2025Article
- Exploring the structural and dynamical features of bacterial-tubulin FtsZ.Biophysical journal · 2025Article
- The geneAntimicrobial agents and chemotherapy · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 2024Article
- Molecular dynamics simulations reveal differences in the conformational stability of FtsZs derived from Staphylococcus aureus and Bacillus subtilis.Scientific reports · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Self-organization of mortal filaments and its role in bacterial division ring formation.Nature physics · 2024Article
- MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.Biomedicines · 2022Review
- FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics.PLoS biology · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism.Nature communications · 2021Article
- The Assembly Switch Mechanism of FtsZ Filament Revealed by All-Atom Molecular Dynamics Simulations and Coarse-Grained Models.Frontiers in microbiology · 2021Article
- Molecular Characterization of theAntibiotics (Basel, Switzerland) · 2020Article
- A Unified Model for Treadmilling and Nucleation of Single-Stranded FtsZ Protofilaments.Biophysical journal · 2020Article
- How Protein Filaments Treadmill.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
FtsZ is the ancestral homolog of tubulin and assembles into the Z ring that organizes the division machinery to drive cell division in most bacteria. In contrast to tubulin that assembles into 13 stranded microtubules that undergo dynamic instability, FtsZ assembles into single-stranded filaments that treadmill to distribute the peptidoglycan synthetic machinery at the septum. Here, using longitudinal interface mutants of FtsZ, we demonstrate that the kinetic polarity of FtsZ filaments is opposite to that of microtubules. A conformational switch accompanying the assembly of FtsZ generates the kinetic polarity of FtsZ filaments, which explains the toxicity of interface mutants that function as a capper and reveals the mechanism of cooperative assembly. This approach can also be employed to determine the kinetic polarity of other filament-forming proteins.
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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.