Spatial regulators for bacterial cell division self-organize into surface waves in vitro.
In the bacterium Escherichia coli, the Min proteins oscillate between the cell poles to select the cell center as division site. This dynamic pattern has been proposed to arise by self-organization of these proteins, and several models have suggested a reaction-diffusion type mechanism. Here, we found that the Min proteins spontaneously formed planar surface waves on a flat membrane in vitro. The formation and maintenance of these patterns, which extended for hundreds of micrometers, required adenosine 5'-triphosphate (ATP), and they persisted for hours. We present a reaction-diffusion model of the MinD and MinE dynamics that accounts for our experimental observations and also captures the in vivo oscillations.
Loose
Martin
M
Biotechnologisches Zentrum der Technischen Universität Dresden, Tatzberg 47-51, 01307 Dresden, Germany.
Fischer-Friedrich
Elisabeth
E
Ries
Jonas
J
Kruse
Karsten
K
Schwille
Petra
P
D000251:Adenosine Triphosphatases / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000502:physiology; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins / Q000502:physiology*; D002455:Cell Division / Q000502:physiology*; D002474:Cell-Free System; D003598:Cytoskeletal Proteins; D004058:Diffusion; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000502:physiology*; D008954:Models, Biological; D009991:Oscillometry
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C093548:MinE protein, E coli; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli