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| Autores principales: | , , |
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| Formato: | Preprint |
| Publicado: |
2024
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| Materias: | |
| Acceso en línea: | https://arxiv.org/abs/2405.17619 |
| Etiquetas: |
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- The tubulin-like protein FtsZ is crucial for cytokinesis in bacteria and many archaea, forming a ring-shaped structure called the Z-ring at the site of cell division. Despite extensive research, the self-assembly of Z-rings is not entirely understood. We propose a theoretical model based on FtsZ's known filament structures, treating them as semiflexible polymers with specific mechanical properties and lateral inter-segment attraction that can stabilize ring formations. Our molecular dynamics simulations reveal various morphological phases, including open helices, chains, rings, and globules, capturing experimental observations in the fission yeast model using FtsZ from different bacterial species or mutants of Escherichia coli. Using our theoretical model, we explore how treadmilling activity affects Z-ring stability and identify a spooling mechanism of ring formation. The active ring produces contractile, shear, and rotational stresses, which intensify as the Z-ring transitions to an open helix at high activity.