title: Protein Patterns and Oscillations on Lipid Monolayers and in Microdroplets.
abstract: The Min proteins from E.coli position the bacterial cell-division machinery through pole-to-pole oscillations. In vitro, Min protein self-organization can be reconstituted in the presence of a lipid membrane as a catalytic surface. However, Min dynamics have so far not been reconstituted in fully membrane-enclosed volumes. Microdroplets interfaced by lipid monolayers were employed as a simple 3D mimic of cellular compartments to reconstitute Min protein oscillations. We demonstrate that lipid monolayers are sufficient to fulfil the catalytic role of the membrane and thus represent a facile platform to investigate Min protein regulated dynamics of the cell-division protein FtsZ-mts. In particular, we show that droplet containers reveal distinct Min oscillation modes, and reveal a dependence of FtsZ-mts structures on compartment size. Finally, co-reconstitution of Min proteins and FtsZ-mts in droplets yields antagonistic localization, thus demonstrating that droplets indeed support the analysis of complex bacterial self-organization in confined volumes.
authors.affiliation: Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.|Developmental Biology, Stanford University, Stanford, CA, 94305, USA.
authors.forename: Katja
authors.initials: K
authors.lastname: Zieske
authors.affiliation: Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Chwastek
authors.affiliation: Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany. schwille@biochem.mpg.de.
authors.forename: Petra
authors.identifier: 0000-0002-6106-4847
authors.initials: P
authors.lastname: Schwille
keywords: biophysics; droplets; membrane proteins; model membranes; protein oscillations