ArticleProceedings of the National Academy of Sciences of the United States of America2012
Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 80 citations in OpenAlex.
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Article
- Stress-mediated growth determinesProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the structural and dynamical features of bacterial-tubulin FtsZ.Biophysical journal · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 2024Article
- Multiple conserved states characterize the twist landscape of the bacterial actin homolog MreB.Computational and structural biotechnology journal · 2022Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis.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
- Targeting the Achilles Heel of FtsZ: The Interdomain Cleft.Frontiers in microbiology · 2021Review
- Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP.mBio · 2020Article
- Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.Annual review of biophysics · 2020Review
- Chiral twisting in a bacterial cytoskeletal polymer affects filament size and orientation.Nature communications · 2020Article
- Surface Orientation and Binding Strength Modulate Shape of FtsZ on Lipid Surfaces.International journal of molecular sciences · 2019Article
- Conservation of conformational dynamics across prokaryotic actins.PLoS computational biology · 2019Article
- Simulations suggest a constrictive force is required for Gram-negative bacterial cell division.Nature communications · 2019Article
- RodZ modulates geometric localization of the bacterial actin MreB to regulate cell shape.Nature communications · 2018Article
- Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Article
- Recent advances in the discovery and development of antibacterial agents targeting the cell-division protein FtsZ.Bioorganic & medicinal chemistry · 2016Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The bacterial cytoskeletal protein FtsZ is a GTPase that is thought to provide mechanical constriction force via an unidentified mechanism. Purified FtsZ polymerizes into filaments with varying structures in vitro: while GTP-bound FtsZ assembles into straight or gently curved filaments, GDP-bound FtsZ forms highly curved filaments, prompting the hypothesis that a difference in the inherent curvature of FtsZ filaments provides mechanical force. However, no nucleotide-dependent structural transition of FtsZ monomers has been observed to support this force generation model. Here, we present a series of all-atom molecular dynamics simulations probing the effects of nucleotide binding on the structure of an FtsZ dimer. We found that the FtsZ-dimer structure is dependent on nucleotide-binding state. While a GTP-bound FtsZ dimer retained a firm monomer-monomer contact, a GDP-bound FtsZ dimer lost some of the monomer-monomer association, leading to a "hinge-opening" event that resulted in a more bent dimer, while leaving each monomer structure largely unaffected. We constructed models of FtsZ filaments and found that a GDP-FtsZ filament is much more curved than a GTP-FtsZ filament, with the degree of curvature matching prior experimental data. FtsZ dynamics were used to estimate the amount of force an FtsZ filament could exert when hydrolysis occurs (20-30 pN per monomer). This magnitude of force is sufficient to direct inward cell-wall growth during division, and to produce the observed degree of membrane pinching in liposomes. Taken together, our data provide molecular-scale insight on the origin of FtsZ-based constriction force, and the mechanism underlying prokaryotic cell division.
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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.