Rice grassy stunt tenuivirus nonstructural protein p5 interacts with itself to form oligomeric complexes in vitro and in vivo

Creators: Chomchan, Pritsana; Li, Shi-Fang; Shirako, Yukio

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).

Additional Information

Copyright © 2003 by the American Society for Microbiology. Received 23 August 2002. Accepted 3 October 2002. We thank Ellen Strauss of the California Institute of Technology for critical reading of the manuscript and Gilda Miranda of the International Rice Research Institute for providing RGSV-infected rice leaves. This work was supported by Grant-in-Aid for Creative Basic Research 09NP0901 from the Ministry of Education, Science, Sports and Culture of Japan. P.C. was supported by a graduate student scholarship from the Ministry of Education, Science, Sports and Culture of Japan. S.-F.L. was supported by a postdoctoral fellowship from the Japan Society for the Promotion of Science.

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