Rice grassy stunt tenuivirus nonstructural protein p5 interacts with itself to form oligomeric complexes in vitro and in vivo.
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).
Chomchan
Pritsana
P
Graduate School of Agricultural Life Sciences, University of Tokyo, Japan.
Li
Shi-Fang
SF
Shirako
Yukio
Y
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*
D004268:DNA-Binding Proteins; C052130:GAL4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D017361:Viral Nonstructural Proteins