Recent in vitro experiments with FtsZ polymers show self-organization into different dynamic patterns, including structures reminiscent of the bacterial Z ring. We model FtsZ polymers as active particles moving along chiral, circular paths by Brownian dynamics simulations and a Boltzmann approach. Our two conceptually different methods point to a generic phase behavior. At intermediate particle densities, we find self-organization into vortex structures including closed rings. Moreover, we show that the dynamics at the onset of pattern formation is described by a generalized complex Ginzburg-Landau equation.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1103/PhysRevLett.116.178301 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Multiscale modelling of active hydrogel elasticity driven by living polymers: softening by bacterial motor protein FtsZ.
Soft Matter
January 2025
Department of Physical Chemistry, Complutense University of Madrid, Av. Complutense s/n, 28040 Madrid, Spain.
Article Synopsis
- The study introduces a neo-Hookean elasticity theory for hybrid mechano-active hydrogels by incorporating motor proteins into polymer structures, leading to materials that actively soften due to adjustable chain overlaps.
- The focus is on polyacrylamide hydrogels enhanced with the bacterial protein FtsZ, using a multiscale model that combines microscopic rubber mesh theory, mesoscopic scaling concepts, and phase transition formalism to explain the observed active softening.
- This research provides valuable insights for designing and controlling complex active hydrogels, potentially advancing applications in technology and biomedicine.
The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.
Nat Commun
September 2024
Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
During bacterial cytokinesis, polymers of the bacterial tubulin FtsZ coalesce into the Z ring to orchestrate divisome assembly and septal cell wall synthesis. Previous studies have found that Z ring condensation and stability is critical for successful cell division. However, how FtsZ filaments condense into a Z ring remains enigmatic and whether septal cell wall synthesis can feedback to the Z ring has not been investigated.
View Article and Find Full Text PDFRole of the antiparallel double-stranded filament form of FtsA in activating the divisome.
mBio
August 2024
Department of Microbiology and Molecular Genetics, UTHealth Houston McGovern Medical School, Houston, Texas, USA.
The actin-like FtsA protein is essential for function of the cell division machinery, or divisome, in many bacteria including . Previous studies demonstrated that purified wild-type FtsA assembles into closed mini-rings on lipid membranes, but oligomeric variants of FtsA such as FtsA and FtsA can bypass certain divisome defects and form arc and double-stranded (DS) oligomeric states, respectively, which may reflect conversion of an inactive to an active form of FtsA. However, it remains unproven which oligomeric forms of FtsA are responsible for assembling and activating the divisome.
View Article and Find Full Text PDFBuilding the Bacterial Divisome at the Septum.
Subcell Biochem
July 2024
Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.
Across living organisms, division is necessary for cell survival and passing heritable information to the next generation. For this reason, cell division is highly conserved among eukaryotes and prokaryotes. Among the most highly conserved cell division proteins in eukaryotes are tubulin and actin.
View Article and Find Full Text PDFGTPase activity regulates FtsZ ring positioning in .
Mol Biol Cell
July 2024
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Bacterial cell division is crucial for replication and requires careful coordination via proteins collectively called the divisome. The tubulin-like GTPase FtsZ is the master regulator of this process and serves to recruit downstream divisome proteins and regulate their activities. Upon assembling at mid-cell, FtsZ exhibits treadmilling motion driven by GTP binding and hydrolysis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!