Reconstituting geometry-modulated protein patterns in membrane compartments

Methods in Cell Biology
Katja Zieske, Petra Schwille

Abstract

The MinCDE protein system from Escherichia coli has become one of the most striking paradigms of protein self-organization and biological pattern formation. The whole set of Min proteins is functionally active to position the divisome machinery by inhibiting Z ring assembly away from mid-cell. This is accomplished by an oscillation behavior between the cell poles, induced by the reaction between the two antagonistic proteins MinD and MinE, which has long caught the attention of quantitative biologists. Technical advances in fluorescence microscopy and molecular biology have allowed us in the past years to reconstitute this MinDE self-organization in cell-free environments on model membranes. We verified the compositional simplicity of protein systems principally required for biological pattern formation, and subjected the mechanism to quantitative biophysical analysis on a single-molecule level. On flat extended membranes, MinD and MinE self-organized into parallel propagating waves. Moreover, employing microsystems technology to construct membrane-clad soft polymer compartments mimicking the shape of native E. coli cells has further enabled us to faithfully reproduce Min protein oscillations. We further investigated the respon...Continue Reading

Citations

Jul 19, 2019·PloS One·Lavisha Jindal, Eldon Emberly

Related Concepts

MinD protein, E coli
MinE protein, E coli
MinC protein, E coli
DNA-dependent ATPase
Cell Division Phases
Plasma Membrane
Cell-Free System
Alkalescens-Dispar Group
Kymography
Cell Surface Proteins

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