A Multistranded Polymer Model Explains MinDE Dynamics in E. coli Cell Division

• Published in: Biophysical journal Vol. 93; no. 4; pp. 1134 - 1150
• Main Authors: Cytrynbaum, Eric N., Marshall, Brandon D.L.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15-08-2007; Biophysical Society; The Biophysical Society
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Binding sites; Biochemistry; Biological Clocks; Biophysical Theory and Modeling; Biopolymers - chemistry; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - genetics; Cell Cycle Proteins - metabolism; Cell Division; Dimerization; Division; Dynamics; E coli; Escherichia coli; Escherichia coli - cytology; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Genotype & phenotype; Microtubules - physiology; Mines; Models, Biological; Mutation; Oscillations; Polymers; Proteins
• ISSN: 0006-3495; 1542-0086
• DOI: 10.1529/biophysj.106.097162

In
Escherichia coli, the location of the site for cell division is regulated by the action of the Min proteins. These proteins undergo a periodic pole-to-pole oscillation that involves polymerization and ATPase activity of MinD under the controlling influence of MinE. This oscillation suppresses division near the poles while permitting division at midcell. Here, we propose a multistranded polymer model for MinD and MinE dynamics that quantitatively agrees with the experimentally observed dynamics in wild-type cells and in several well-studied mutant phenotypes. The model also provides new explanations for several phenotypes that have never been addressed by previous modeling attempts. In doing so, the model bridges a theoretical gap between protein structure, biochemistry, and mutant phenotypes. Finally, the model emphasizes the importance of nonequilibrium polymer dynamics in cell function by demonstrating how behavior analogous to the dynamic instability of microtubules is used by
E. coli to achieve a sufficiently rapid timescale in controlling division site selection.