title: Mapping of the regions involved in self-interaction of rice stripe virus P3 protein.
abstract: Rice stripe virus (RSV) protein P3 is a suppressor of RNA silencing in plants. P3 has been shown by biomolecular fluorescence complementation assay to self-interact in planta but the regions responsible for homotypic interaction have not been determined. Here we analyzed the domains for the self-interaction of P3 by using yeast two-hybrid, co-immunoprecipitation and fluorescence experiments. The results showed that P3 was also able to interact with itself in yeast and insect cells. The domain responsible for P3-P3 interaction was mapped to amino acids 15-30 at the N-terminal region of P3. Furthermore, subcellular localization suggested that the homo-oligomerization was the prerequisite for P3 to form larger protein aggregates in the nucleus of insect cell.
authors.forename: S L
authors.initials: SL
authors.lastname: Zhao
authors.forename: J H
authors.initials: JH
authors.lastname: Hao
authors.forename: Y N
authors.initials: YN
authors.lastname: Xue
authors.forename: C Y
authors.initials: CY
authors.lastname: Liang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D018411:Spodoptera / Q000821:virology; D029364:Tenuivirus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D014764:Viral Proteins
keywords: rice stripe virus; P3; self-interaction; yeast two-hybrid; co-immunoprecipitation.