title: Studies on interaction of cucurbit aphid-borne yellow virus proteins using yeast two-hybrid system and bimolecular fluorescence complementation.
abstract: In this article, yeast two-hybrid system (YTHS) and bimolecular fluorescence complementation (BiFC) were used to analyze the interactions of cucurbit aphid-borne yellows virus (CABYV)-encoded proteins. P0, P1, P1-2, P3, P4, and P5 were tested by YTHS in all possible pairwise combinations, and only P3/P3 interaction was detected. Results obtained by BiFC further confirmed the self-interaction of P3, and the subcellular localization of reconstituted YFP fluorescence was observed mainly in nuclei of Nicotiana benthamiana leaf epidermal cells. Domains involved in P3/P3 self-interaction were analyzed by YTHS and BiFC using deletion mutants. The results showed that R domain (residues 1-61) in the N-terminus could self-interact, and it also interacted with the S domain (residues 62-199) in the C-terminus of P3. The present work would serve as a molecular basis for further characterization of CABYV proteins, and the regions involved in P3/P3 self-interaction could provide the clue for understanding the capsid assembly pathway of CABYV.
authors: China Agricultural University, Beijing, People's Republic of China.
authors: X H
authors: XH
authors: Chen
authors: H Y
authors: HY
authors: Xiang
authors: Z
authors: Z
authors: Wang
authors: Y J
authors: YJ
authors: Zhang
authors: C G
authors: CG
authors: Han
authors: D W
authors: DW
authors: Li
authors: J L
authors: JL
authors: Yu
authors: Y Q
authors: YQ
authors: Cheng
mesh_terms: D005453:Fluorescence; D052679:Luteoviridae / Q000378:metabolism*; D010957:Plasmids; D025941:Protein Interaction Mapping / Q000379:methods; D014026:Nicotiana / Q000378:metabolism / Q000821:virology; D020798:Two-Hybrid System Techniques; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D014764:Viral Proteins