Functional Analysis Of Protein Verprolin MoVrp1 In Magnaporthe Oryzae

Rice blast fungus,Magnaporthe oryzae,is an important model organism for the study of fungal growth,development and pathogenic mechanism.Actin is a major component of the cytoskeleton in all eukaryotic cells.Actin cytoskeleton plays a central role in many cell biological processes.The WH2 domain is an ancient actin monomer-binding motif,that is found in many different regulators of the actin cytoskeleton.Vrplp is a proline-rich protein which is essential for cytokinesis and for normal actomyosin ring assembly.Vrplp which localizes to the cortical actin cytoskeleton,is necessary for its polarization to sites of growth and for endocytosis.In S.cerevisiae,Vrpl-Lasl7-Rvs167 is a "scaffold" structure.But in the M.oryzae,there was no obvious interaction phenomenon between MoVrpl and MoLas17 or MoRvs167.In order to detect the function of MoVrp1,we got the deletion mutant Movrp1.Compared with the wild type strains,we found that the growth rate of the deletion mutant decreased dramatically.There is no conidium formation in the deletion mutant.Moreover,the deletion mutant lost the pathogenicity when inoculating on leaves of barley and rice.These results showed that MoVrp1 is closely related with pathogenic process of the rice blast fungus,the conidium formation and the growth process.