title: Pattern formation within Escherichia coli: diffusion, membrane attachment, and self-interaction of MinD molecules.
abstract: In E. coli, accurate cell division depends upon the oscillation of Min proteins from pole to pole. We provide a model for the polar localization of MinD based only on diffusion, a delay for nucleotide exchange, and different rates of attachment to the bare membrane and the occupied membrane. We derive analytically the probability density, and correspondingly the length scale, for MinD attachment zones. Our simple analytical model illustrates the processes giving rise to the observed localization of cellular MinD zones.
authors.affiliation: NEC Laboratories America, Inc., Princeton, New Jersey 08540, USA. kulkarni@vt.edu
authors.forename: Rahul V
authors.initials: RV
authors.lastname: Kulkarni
authors.forename: Kerwyn Casey
authors.initials: KC
authors.lastname: Huang
authors.forename: Morten
authors.initials: M
authors.lastname: Kloster
authors.forename: Ned S
authors.initials: NS
authors.lastname: Wingreen
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D003198:Computer Simulation; D004058:Diffusion; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008561:Membrane Fusion / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D015233:Models, Statistical; D011485:Protein Binding; D021381:Protein Transport / Q000502:physiology*
chemical_list: D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli