Round Table Seminar - Thorsten Seidel, Frommer Lab, What does FRET tell us about protein-interactions?

The activities of many, if not all, enzymes depend on the formation of complexes and the modulation by protein-protein interactions. Most binding mechanisms and the required conditions of interaction can be characterized in vitro, e.g. by the estimation of binding affinities, but the data’s significance for the cell often remains elusive. Additional proteins likely have an impact on complex-formation. Also the spatial as well temporal distribution of the interaction partners has to be considered. Here, the improvement and engineering of fluorescent proteins enables quantitative imaging of protein-protein interactions and thus, addressing this issue in the living plant cell, either by bimolecular fluorescence complementation (BiFC) or by Foerster resonance energy transfer (FRET). My recent work on the choice of FRET-pairs based on their bio-physical properties, the detection of oligomeric complexes, and the application of photo-switchable fluorescent proteins for FRET will be summarized in the seminar