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Journal of Virology, January 2003, p. 769-775, Vol. 77, No. 1
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.1.769-775.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Shi-Fang Li,2,
and Yukio Shirako2*
Graduate School of Agricultural Life Sciences,1 Asian Center for Bioresources and Environmental Sciences (ANESC), University of Tokyo, Tokyo, Japan2
Received 23 August 2002/ Accepted 3 October 2002
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).
Present address: Division of Biology, California Institute of Technology, Pasadena, CA 91125.
Present address: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Science, Beijing 100094, People's Republic of China.
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