Related Experiment Video
Updated: Jul 3, 2026

FtsZ Polymerization Assays: Simple Protocols and Considerations
Published on: November 16, 2013
Polymerization and bundling kinetics of FtsZ filaments
Ganhui Lan1, Alex Dajkovic, Denis Wirtz
1Department of Mechanical Engineering, The Johns Hopkins University, Baltimore, Maryland, USA.
Abstract:
FtsZ is a tubulin homolog essential for prokaryotic cell division. In living bacteria, FtsZ forms a ringlike structure (Z-ring) at the cell midpoint. Cell division coincides with a gradual contraction of the Z-ring, although the detailed molecular structure of the Z-ring is unknown. To reveal the structural properties of FtsZ, an understanding of FtsZ filament and bundle formation is needed. We develop a kinetic model that describes the polymerization and bundling mechanism of FtsZ filaments. The model reveals the energetics of the FtsZ filament formation and the bundling energy between filaments. A weak lateral interaction between filaments is predicted by the model. The model is able to fit the in vitro polymerization kinetics data of another researcher, and explains the cooperativity observed in FtsZ kinetics and the critical concentration in different buffer media. The developed model is also applicable for understanding the kinetics and energetics of other bundling biopolymer filaments.
Related Concept Videos
Actin Polymerization
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
Formation of Intermediate Filaments
Assembly of Cytoskeletal Filaments
Formation of Higher-order Actin Filaments
The high-order actin networks...
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

