Abstract
Pathogens dispatch numerous proteins called effector to plant cells to disturb plant defense responses. On the other hand, plants recognize the effectors and induce strong defense responses including the oxidative burst and programmed cell death. Although the genes involved in the plant-pathogen interactions have been identified, little is known about the mechanisms of the effector recognition and of the subsequent signal transduction. It is especially difficult to study the function of effectors because the amino acid sequences are not highly conserved. To elucidate the molecular basis for the mechanism of interaction between effectors and plant defense-related proteins, we study the three-dimensional structure of proteins by X-ray crystallography and NMR spectroscopy. We screened for proteins which were highly expressed and soluble by using the high-throughput cell-free protein expression system.
