title: Rice grassy stunt tenuivirus nonstructural protein p5 interacts with itself to form oligomeric complexes in vitro and in vivo.
abstract: We investigated the interaction of Rice grassy stunt tenuivirus (RGSV) nonstructural protein p5, a protein of 22 kDa encoded on vRNA 5, with all 12 RGSV proteins by using a GAL4 transcription activator-based yeast two-hybrid system. The p5 protein interacted only with itself and not with any other viral protein; the interacting domains were localized within the N-terminal 96 amino acids of p5. The p5-p5 interaction was reproduced in an Sos recruitment-mediated yeast two-hybrid system as well in by far-Western blots. Native p5 protein extracted from RGSV-infected rice tissue was detected in a large complex with a molecular mass of approximately 260 kDa composed of 12 molecules of p5 or a p5 oligomer with an unidentified host factor(s).
authors.affiliation: Graduate School of Agricultural Life Sciences, University of Tokyo, Japan.
authors.forename: Pritsana
authors.initials: P
authors.lastname: Chomchan
authors.forename: Shi-Fang
authors.initials: SF
authors.lastname: Li
authors.forename: Yukio
authors.initials: Y
authors.lastname: Shirako
mesh_terms: D015153:Blotting, Western; D004268:DNA-Binding Proteins; D008970:Molecular Weight; D012275:Oryza / Q000821:virology*; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics; D029364:Tenuivirus / Q000737:chemistry*; D014157:Transcription Factors / Q000235:genetics; D020798:Two-Hybrid System Techniques; D017361:Viral Nonstructural Proteins / Q000032:analysis / Q000737:chemistry*
chemical_list: D004268:DNA-Binding Proteins; C052130:GAL4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D017361:Viral Nonstructural Proteins