A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement.
Determination of the proper site for division in Escherichia coli and other bacteria involves a unique spatial oscillatory system in which membrane-associated structures composed of the MinC, MinD and MinE proteins oscillate rapidly between the two cell poles. In vitro evidence indicates that this involves ordered cycles of assembly and disassembly of MinD polymers. We propose a mathematical model to explain this behavior. Unlike previous attempts, the present approach is based on the expected behavior of polymerization-depolymerization systems and incorporates current knowledge of the biochemical properties of MinD and MinE. Simulations based on the model reproduce all of the known topological and temporal characteristics of the in vivo oscillatory system.
Drew
Donald A
DA
Department of Mathematical Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180-3590, USA.
Osborn
Mary J
MJ
Rothfield
Lawrence I
LI
D000251:Adenosine Triphosphatases / Q000502:physiology; D001419:Bacteria / Q000166:cytology*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000502:physiology; D018797:Cell Cycle Proteins; D002455:Cell Division / Q000502:physiology*; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D016764:Cell Polarity; D003198:Computer Simulation; D003593:Cytoplasm / Q000502:physiology / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000502:physiology; D008433:Mathematics; D008954:Models, Biological; D009991:Oscillometry
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C080466:MinC protein, Bacteria; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli