The enterobacterial Rcs phosphorelay system is an advanced and multivalent prokaryotic signal transduction pathway that has originated from the classical two-component system. Its exceptional structural complexity involving accessory modulators, unique subclasses of phosphoreceiver domains and phosphorylation-induced structural rearrangements correlates with its participation in diverse regulation circuits affecting capsule biosynthesis, motility, virulence, cell-division and many others. We combine high resolution NMR techniques with biochemical and microbiological assays for the concerted structural and functional analysis of the individual Rcs signalling components. Our strategy focuses in particular on structural dynamic effects and on the modulation of protein binding interfaces by phosphorylation of individual interaction partners. Formation of protein complexes within the signalling chain will be analysed based on our NMR structures of individual interaction partners and we will further complete the molecular picture of the Rcs system by solving structures of still lacking components. The expected results will deliver a comprehensive view of Rcs phosphorelay mechanisms comprising structural details as well as insights into dynamic conformational rearrangements during the signalling processes.
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- Rogov, V.V., Schmöe, K., Löhr, F., Rogova, N.Y., Bernhard, F. & Dötsch, V. Modulation of the Rcs-mediated signal transfer by conformational flexibility.Biochem. Soc. Trans., 36, 1427-1432(2008)