Abstract
The bacterial flagellum is a marvel of Nature. Composed of thousands of proteins, it propels its host using only a set of 6 kinds of proteins, assembled into the basal body. In vivo and in vitro studies revealed some aspect of it, in term of mechanical efficiency; proteins structures and part of its mechanism were highlighted by large-scale mutagenesis. However, a precise description of the motor's mechanism remains to be established. We report the use of cell free expression of several motor proteins, expressed into a “proteocell”. A cell free system has been encapsulated into a lipid bilayer, forming a vesicle reactor-cell. By tracking the localization of the proteins using a fluorescence tag, 6 basal body proteins FliF, FliG, FliM FliN MotA and MotB were localized. In order to validate our approach, interaction between FliF and FliG was studied and confirmed by the use of truncated mutants of FliG showing no affinity for FliF. These results represent a novel and ambitious approach for studying in vitro complex architecture machinery as the flagellum nanomotor.View Large Image | View Hi-Res Image | Download PowerPoint Slide
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