Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.
Proper cell division requires an accurate definition of the division plane. In bacteria, this plane is determined by a polymeric ring of the FtsZ protein. The site of Z ring assembly in turn is controlled by the Min system, which suppresses FtsZ polymerization at noncentral membrane sites. The Min proteins in Escherichia coli undergo a highly dynamic localization cycle, during which they oscillate between the membrane of both cell halves. By using computer simulations we show that Min protein dynamics can be described accurately by using the following assumptions: (i) the MinD ATPase self-assembles on the membrane and recruits both MinC, an inhibitor of Z ring formation, and MinE, a protein required for MinC/MinD oscillation, (ii) a local accumulation of MinE is generated by a pattern formation reaction that is based on local self-enhancement and a long range antagonistic effect, and (iii) it displaces MinD from the membrane causing its own local destabilization and shift toward higher MinD concentrations. This local destabilization results in a wave of high MinE concentration traveling from the cell center to a pole, where it disappears. MinD reassembles on the membrane of the other cell half and attracts a new accumulation of MinE, causing a wave-like disassembly of MinD again. The result is a pole-to-pole oscillation of MinC/D. On time average, MinC concentration is highest at the poles, forcing FtsZ assembly to the center. The mechanism is self-organizing and does not require any other hypothetical topological determinant.
Meinhardt
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Max-Planck-Institut für Entwicklungsbiologie, Spemannstrasse 35, D-72076 Tübingen, Germany. Hans.Meinhardt@tuebingen.mpg.de
de Boer
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PA
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D002455:Cell Division / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity / Q000502:physiology; D003198:Computer Simulation; D003598:Cytoskeletal Proteins; D004926:Escherichia coli / Q000166:cytology* / Q000254:growth & development / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008954:Models, Biological
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C080466:MinC protein, Bacteria; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli