Related Experiment Video
Updated: Apr 11, 2026

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
Published on: July 28, 2018
Molecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing
James C Walsh1, Christopher N Angstmann2, Iain G Duggin3
1School of Physics, University of New South Wales, Sydney NSW 2052, Australia; The ithree institute, University of Technology, Sydney NSW 2007, Australia.
Abstract:
Oscillations of the Min protein system are involved in the correct midcell placement of the divisome during Escherichia coli cell division. Based on molecular interactions of the Min system, we formulated a mathematical model that reproduces Min patterning during cell growth and division. Specifically, the increase in the residence time of MinD attached to the membrane as its own concentration increases, is accounted for by dimerisation of membrane-bound MinD and its interaction with MinE. Simulation of this system generates unparalleled correlation between the waveshape of experimental and theoretical MinD distributions, suggesting that the dominant interactions of the physical system have been successfully incorporated into the model. For cells where MinD is fully-labelled with GFP, the model reproduces the stationary localization of MinD-GFP for short cells, followed by oscillations from pole to pole in larger cells, and the transition to the symmetric distribution during cell filamentation. Cells containing a secondary, GFP-labelled MinD display a contrasting pattern. The model is able to account for these differences, including temporary midcell localization just prior to division, by increasing the rate constant controlling MinD ATPase and heterotetramer dissociation. For both experimental conditions, the model can explain how cell division results in an equal distribution of MinD and MinE in the two daughter cells, and accounts for the temperature dependence of the period of Min oscillations. Thus, we show that while other interactions may be present, they are not needed to reproduce the main characteristics of the Min system in vivo.
Insights
The Min protein system ensures proper cell division in Escherichia coli. A new mathematical model accurately simulates Min protein oscillations and localization, revealing key molecular interactions for cell division.
Area of Science:
- Cell Biology
- Biophysics
- Mathematical Biology
Background:
- The Min protein system regulates cell division placement in Escherichia coli.
- Understanding Min system dynamics is crucial for comprehending bacterial cell division.
Purpose of the Study:
- To develop a mathematical model of the Min protein system.
- To simulate Min patterning and protein localization during cell division.
- To identify key molecular interactions governing Min system behavior.
Main Methods:
- Formulation of a mathematical model based on known Min protein interactions.
- Computer simulations of MinD and MinE dynamics in Escherichia coli.
- Comparison of model predictions with experimental data for MinD-GFP localization.
Main Results:
- The model accurately reproduces MinD waveshape and localization patterns, including oscillations and midcell placement.
- Simulations account for differences in MinD localization based on labeling.
- The model explains the temperature dependence of Min oscillations and equal Min protein distribution in daughter cells.
Conclusions:
- The developed mathematical model successfully captures essential Min system dynamics in vivo.
- Key molecular interactions, such as MinD dimerization and MinE interaction, are sufficient to explain Min patterning.
- The model provides insights into the physical basis of bacterial cell division regulation.
Related Concept Videos
Cytoskeletal Proteins in Bacteria
Stringent Response in E. coli
Chemotaxis in E. coli
Coordination of Gene Expression Processes in Bacteria
Replication in Prokaryotes
Replication in Prokaryotes
Many Proteins Work Together to Replicate the Chromosome
Replication is coordinated and carried out by a host of specialized...

