Interaction Between P2 Of Rice Stripe Virus And Cajal Body

Rice stripe disease,caused by rice stripe virus(RSV),is a significant rice diseases,which decreases rice production and is called“rice cancer”.RSV is a typical member of the genus Tenuivirus.The pathogenesis and protein function of RSV are research hotspots.p2,a significant protein of RSV,interacts with Nicotiana benthamiana fibrillan2(Nb Fib2)and involves in virus infection.Nb Fib2 localizes in nucleolus and cajal bodies.This thesis takes advantage that p2 is a nucleoplasm shuttle protein and Nicotiana benthamiana can be infected by RSV,the interaction between p2 and N.benthamiana coilin(Nbcoilin)is dissected.The results provide scientific a basis for understanding the biological function of p2 and Nbcoilin.This thesis comprises two sections.1.The full-length of Nbcoilin is achieved firstly.Based on the blast results of Arabidopsis thaliana coilin against Nicotiana benthamiana genome database,the primers are designed for PCR,then amplify the putative full-length of Nbcoilin by 5’-race and 3’-race.The full-length of it is 3,017 bp,the complete coding region is 2,409 bp in length,encoding802 amino acids.The online softs show it contains three typical functional domains of coilin protein and a “tudor” region.The homology of amino acid between Nbcoilin and other plant coilins are more than50%.Phylogenetic analysis showed that the Nbcoilin was placed in a cluster with other plant coilins.The subcellular localization analysis showed Nbcoilin co-localizes with Atcoilin.These results indicated that the cloned Nbcoilin gene is a homologous protein of coilin.2.The relationship between p2 and Nbcoilin.Co-localization and Bi FC assays shows p2 binds to Nbcoilin.The gene of Nbcoilin is silenced by using VIGS method.Those silenced-plants shows typical symptoms after inoculated by RSV.RSV can be detected by RT-PCR and western blot.It indicates that Nbcoilin fails to affect RSV infection.Thus,Nbcoilin maybe just help p2 go into and out nucleus,the results lay a foundation for further studying of the interaction between p2 and Nbcoilin.