title: Surface topology assisted alignment of Min protein waves.
abstract: Self-organization of proteins into large-scale structures is of pivotal importance for the organization of cells. The Min protein system of the bacterium Escherichia coli is a prime example of how pattern formation occurs via reaction-diffusion. We have previously demonstrated how Min protein patterns are influenced by compartment geometry. Here we probe the influence of membrane surface topology, as an additional regulatory element. Using microstructured membrane-clad soft polymer substrates, Min protein patterns can be aligned. We demonstrate that Min pattern alignment starts early during pattern formation and show that macroscopic millimeter-sized areas of protein patterns of well-defined orientation can be generated.
authors.affiliation: Dept. Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Katja
authors.initials: K
authors.lastname: Zieske
authors.affiliation: Dept. Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Jakob
authors.initials: J
authors.lastname: Schweizer
authors.affiliation: Dept. Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. Electronic address: schwille@biochem.mpg.de.
authors.forename: Petra
authors.initials: P
authors.lastname: Schwille
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D004058:Diffusion; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D053835:Unilamellar Liposomes / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D053835:Unilamellar Liposomes; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli
keywords: Diffusion–reaction mechanism; MinD; MinE; Pattern formation; Self-organization