A mechanism for polar protein localization in bacteria.
We investigate a mechanism for the polar localization of proteins in bacteria. We focus on the MinCD/DivIVA system regulating division site placement in the rod-shaped bacterium Bacillus subtilis. Our model relies on a combination of geometric effects and reaction-diffusion dynamics to direct proteins to both cell poles, where division is then blocked. We discuss similarities and differences with related division models in Escherichia coli and also develop extensions of the model to asymmetric polar protein localization. We propose that our mechanism for polar localization may be employed more widely in bacteria, especially in outgrowing spores, which do not possess any pre-existing polar division apparatus from prior division events.
Howard
Martin
M
Department of Mathematics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
D000251:Adenosine Triphosphatases / Q000502:physiology*; D001412:Bacillus subtilis / Q000502:physiology*; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins / Q000502:physiology*; D002455:Cell Division / Q000502:physiology*; D016764:Cell Polarity / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000502:physiology*; D008954:Models, Biological
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; C104636:DivIVA protein, bacteria; D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli