Abstract

Dynamic protein oscillations spatially regulate the localization of the division site in the bacterium Escherichia coli. The pole-to-pole oscillations of Min proteins result on time-average in a nonhomogeneous protein concentration profile with the highest concentration at the cell poles, where cell division is inhibited.Aiming at understanding spatial organization during cell division on the scale of individual molecules we reconstituted a system of self-organizing Min proteins in artificial micro compartments in a bottom-up approach. Using a devise composed of PDMS micro compartments, supported lipid bilayers and purified proteins we engineered a biomimetic minimal system in which the dynamic oscillations of Min proteins were reconstituted in vitro [1]. By systematically varying the shape of the micro compartments, this biomimetic system enables us to investigate how compartment geometry influences pattern formation of a self-organizing protein system in vitro. Furthermore this system provides a platform to study protein gradient formation of the Min system and Min protein regulated localization of downstream proteins in a well-defined environment.[1] Zieske, K. and Schwille, P. (2013), Reconstitution of Pole-to-Pole Oscillations of Min Proteins in Microengineered Polydimethylsiloxane Compartments. Angew Chem Int Ed Engl. 52: 459-462.

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