Chomchan, Pritsana and Li, Shi-Fang and Shirako, Yukio (2003) Rice grassy stunt tenuivirus nonstructural protein p5 interacts with itself to form oligomeric complexes in vitro and in vivo. Journal of Virology, 77 (1). pp. 769-775. ISSN 0022-538X. http://resolver.caltech.edu/CaltechAUTHORS:CHOjvir03
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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.|
|Subject Keywords:||GENUS TENUIVIRUS; 2-HYBRID SYSTEM; VIRUS; SOS|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||20 Jul 2006|
|Last Modified:||26 Dec 2012 08:57|
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