ArticleBiopolymers2016
Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.
Article in Biopolymers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Stress-mediated growth determinesProceedings of the National Academy of Sciences of the United States of America · 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
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- 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
- Self-organization of mortal filaments and its role in bacterial division ring formation.Nature physics · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers.Open biology · 2023Article
- FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.Nature communications · 2022Article
- Targeting the Achilles' Heel of Multidrug-ResistantInternational journal of molecular sciences · 2022Article
- A pairwise distance distribution correction (DDC) algorithm to eliminate blinking-caused artifacts in SMLM.Nature methods · 2021Article
- A two-track model for the spatiotemporal coordination of bacterial septal cell wall synthesis revealed by single-molecule imaging of FtsW.Nature microbiology · 2021Article
- FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division.Nature communications · 2021Article
- Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates.Biochimica et biophysica acta. Molecular cell research · 2021Article
- Ectopic positioning of the cell division plane is associated with single amino acid substitutions in the FtsZ-recruiting SsgB inOpen biology · 2021Article
- Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.Annual review of biophysics · 2020Review
- FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus.Journal of bacteriology · 2020Article
- At the Heart of Bacterial Cytokinesis: The Z Ring.Trends in microbiology · 2019Review
- Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Biophysical journal · 2017Article
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4 authors.
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Abstract
FtsZ is an essential bacterial cytoskeletal protein that assembles into a ring-like structure (Z-ring) at midcell to carry out cytokinesis. In vitro, FtsZ exhibits polymorphism in polymerizing into different forms of filaments based on its GTPase activity, concentration, and buffer condition. In vivo, the Z-ring appeared to be punctate and heterogeneously organized, although continuous, homogenous Z-ring structures have also been observed. Understanding how the Z-ring is organized in vivo is important because it provides a structural basis for the functional role of the Z-ring in cytokinesis. Here, we assess the effects of both GTPase activity and FtsZ concentration on the organization of the Z-ring in vivo using three-dimensional (3D) superresolution microscopy. We found that the Z-ring became more homogenous when assembled in the presence of a GTPase-deficient mutant, and upon overexpression of either wt or mutant FtsZ. These results suggest that the in vivo organization of the Z-ring is largely dependent on the intrinsic polymerization properties of FtsZ, which are significantly influenced by the GTPase activity and concentration of FtsZ. Our work provides a unifying theme to reconcile previous observations of different Z-ring structures, and supports a model in which the wt Z-ring comprises loosely associated, heterogeneously distributed FtsZ clusters. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 725-734, 2016.
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