Identification of Functional Domain(s) of Fibrillarin Interacted with p2 of Rice stripe virus. (15th March 2018)

• Record Type: Journal Article
• Authors: Zheng, Luping; He, Jie; Ding, Zuomei; Zhang, Chenlong; Meng, Ruoxue
• Other Names: Yang Jialiang Academic Editor.
• Is Part Of: Canadian journal of infectious diseases & medical microbiology =. Volume 2018(2018)
• Publication Date: 2018-03-15
• Subjects: Communicable diseases -- Periodicals; Infection -- Periodicals; Communicable diseases; Infection; Communicable Diseases; Communicable Disease Control; Electronic journals; Periodicals; Fulltext; Internet Resources; Periodicals; 616.9
• DOI: 10.1155/2018/8402839
• Languages: English
• ISSNs: 1712-9532

Abstract

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).