Preliminary Crystallographic Study Of Salicylic Acid Receptor NPR4

Phytohormone salicylic acid(SA),which promotes the expression of pathogenesis related protein and actives plant defense mechanisms,could increase systemic acquired resistance and play an indispensable role on resistance to pathogens in host.Recent reports showed that NPR4(nonexpresser of pathogenesis related genes 4)is a potential receptor for salicylic acid that could mediate transcription of pathogenesis related gene.NPR4 contains three domains: BTB/POZ domain,ANK domain and substrate binding domain.BTB/POZ domain participates in the interaction between NPR4 and transcription factor TGA,which is related in protein degradation and cytoskeleton regulation,and is the main executive in NPR4 functions.In this study,we taked tools for molecular biology to establish a series of recombinant plasmid consist of full-length protein,mutant of core domain and pathogenesis related,with that,we build protein purification scheme.Finally,We carry out the research of protein characterization and structural analysis via crystallographic method,and we obtain a variety of crystal.The preliminary diffraction analysis indicates that the crystal resolution is around 8?,which provides a structural basis for the subsequent study about NPR4 signal transduction mechanism.