Structural and biochemical characterisation of plant EDS1 disease resistance regulatory complexes

• Antragstellerinnen / Antragsteller: Professor Dr. Karsten Niefind; Professorin Dr. Jane E. Parker
• Fachliche Zuordnung: Biochemie und Biophysik der Pflanzen
• Förderung: Förderung von 2007 bis 2011
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 39953024

In plants, the nucleo-cytoplasmic protein EDS1 and its interacting partners PAD4 and SAG101 control the induction of defences and programmed cell death against invasive pathogens. Here, we aim in a collaborative project to elucidate the biochemical and molecular mechanisms by which EDS1 complexes transduce signals inside the cell. Although EDS1 and its partners have sequence similarities to lipases, our genetical and biochemical data reveal that they are not acyl hydrolase enzymes. Instead, we have evidence of a lipid reducing activity by EDS1 and have identified sequence motifs that could mediate lipid binding. We have developed protocols to purify large quantitities of soluble Arabidopsis EDS1 alone or complexed with PAD4 or SAG101 from E.coli. We will use the pure proteins to determine the physico-chemical and kinetic properties of EDS1 complexes, intensify crystallisation experiments and further characterize EDS1 enzymatic and lipid binding capabilities. Data produced should provide a new dimension and direction to understanding intrinsic protein functions in the plant defence signalling network.

• DFG-Verfahren: Sachbeihilfen