Abstract
p2 of Rice stripe virus may promote virus systemic infection by interacting with the full length of fibrillarin from Nicotiana benthamiana (NbFib2) in the nucleolus and cajal body (CB). NbFib2 contains three functional domains. We used yeast two-hybrid, colocalization, and bimolecular fluorescence complementation (BiFC) assays to study the interactions between p2 and the three domains of NbFib2, namely, the N-terminal fragment containing a glycine and arginine-rich (GAR) domain, the central RNA-binding domain, and the C-terminal fragment containing an α-helical domain. The results show that the N-terminal domain is indispensable for NbFib2 to localize in the nucleolus and cajal body. p2 binds all three regions of NbFib2, and they target to the nucleus but fail to the nucleolus and cajal bodies (CBs).
Highlights
Rice stripe virus (RSV), an economically significant pathogen of rice, is the member of the genus Tenuivirus
RNA3 encodes a nonstructural protein p3, another suppressor of gene silencing [11], and a structural protein pc3, which is a nucleocapsid protein connected with resistance to RSV [12, 13]. e nonstructural disease-specific protein (SP) and the movement protein pc4 are encoded by RNA4 [14, 15]
We found that p2 of RSV targeted to NbFib2 to promote virus systemic movement [8]
Summary
Rice stripe virus (RSV), an economically significant pathogen of rice, is the member of the genus Tenuivirus. NbFib2-1: N-terminal fragment from 1 aa to 130 aa, containing a GAR region and a glycine- and arginine-rich domain. NbFib2-2: the central RNA-binding domain from 131 aa to 221 aa.
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