ArticleProceedings of the National Academy of Sciences of the United States of America2012
Depolymerization dynamics of individual filaments of bacterial cytoskeletal protein FtsZ.
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 25 papers.
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Who cites it
25 citing papers in PubMed.
- Visualizing the dynamic polymerization of the bacterial actin-like cytoskeleton for magnetic organelle positioning.Scientific reports · 2025Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- Dynamic Assembly/Disassembly ofInternational journal of molecular sciences · 2021Article
- A stochastic model for dynamics of FtsZ filaments and the formation of Z -ring.The European physical journal. E, Soft matter · 2020Article
- Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.Annual review of biophysics · 2020Review
- Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.Journal of molecular biology · 2020Article
- Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.mBio · 2018Article
- Turgor Pressure and Possible Constriction Mechanisms in Bacterial Division.Frontiers in microbiology · 2018Review
- Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Biophysical journal · 2017Article
- Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein.Scientific reports · 2016Article
- Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.Biopolymers · 2016Article
- Efficient Multiscale Models of Polymer Assembly.Biophysical journal · 2016Article
- Defining the rate-limiting processes of bacterial cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves.Biophysical journal · 2015Article
- FtsZ filament capping by MciZ, a developmental regulator of bacterial division.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity.PloS one · 2015Article
- Understanding nucleotide-regulated FtsZ filament dynamics and the monomer assembly switch with large-scale atomistic simulations.Biophysical journal · 2014Article
- Divided we stand: splitting synthetic cells for their proliferation.Systems and synthetic biology · 2014Review
- MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns.Nature cell biology · 2014Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report observation and analysis of the depolymerization filaments of the bacterial cytoskeletal protein FtsZ (filament temperature-sensitive Z) formed on a mica surface. At low concentration, proteins adsorbed on the surface polymerize forming curved filaments that close into rings that remain stable for some time before opening irreversibly and fully depolymerizing. The distribution of ring lifetimes (T) as a function of length (N), shows that the rate of ring aperture correlates with filament length. If this ring lifetime is expressed as a bond survival time, (T(b) ≡ NT), this correlation is abolished, indicating that these rupture events occur randomly and independently at each monomer interface. After rings open irreversibly, depolymerization of the remaining filaments is fast, but can be slowed down and followed using a nonhydrolyzing GTP analogue. The histogram of depolymerization velocities of individual filaments has an asymmetric distribution that can be fit with a computer model that assumes two rupture rates, a slow one similar to the one observed for ring aperture, affecting monomers in the central part of the filaments, and a faster one affecting monomers closer to the open ends. From the quantitative analysis, we conclude that the depolymerization rate is affected both by nucleotide hydrolysis rate and by its exchange along the filament, that all monomer interfaces are equally competent for hydrolysis, although depolymerization is faster at the open ends than in central filament regions, and that all monomer-monomer interactions, regardless of the nucleotide present, can adopt a curved configuration.
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