Min-protein oscillations in Escherichia coli with spontaneous formation of two-stranded filaments in a three-dimensional stochastic reaction-diffusion model.
We introduce a three-dimensional stochastic reaction-diffusion model to describe MinD/MinE dynamical structures in Escherichia coli. This model spontaneously generates pole-to-pole oscillations of the membrane-associated MinD proteins, MinE ring, as well as filaments of the membrane-associated MinD proteins. Experimental data suggest MinD filaments are two-stranded. In order to model them we assume that each membrane-associated MinD protein can form up to three bonds with adjacent membrane-associated MinD molecules and that MinE induced hydrolysis strongly depends on the number of bonds MinD has established.
Pavin
Nenad
N
Department of Physics, Faculty of Science, University of Zagreb, Zagreb, Croatia.
Paljetak
Hana Cipcić
HC
Krstić
Vladimir
V
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D001683:Biological Clocks / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D003198:Computer Simulation; D004058:Diffusion; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D013269:Stochastic Processes
D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C076835:FtsZ84 protein, E coli; D008565:Membrane Proteins; C462942:MinC protein, E coli; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli