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The Arginine-Rich Motif of Bamboo mosaic virus Satellite RNA-Encoded P20 Mediates Self-Interaction, Intracellular Targeting, and Cell-to-Cell Movement

July 2006 , Volume 19 , Number  7
Pages  758 - 767

Paramasivan Vijaya Palani , 1 Venkatraman Kasiviswanathan , 1 Jeff Chien-Fu Chen , 1 Wei Chen , 2 Yau-Heiu Hsu , 2 and Na-Sheng Lin 1

1Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan 115; 2Graduate Institute of Biotechnology, National Chung Hsing University, Taichung, Taiwan 402, Republic of China


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Accepted 14 February 2006.

Satellite RNA of Bamboo mosaic virus (satBaMV) has a single open reading frame for a nonstructural, RNA-binding protein, P20, which facilitates the long-distance movement of satBaMV in Nicotiana benthamiana. Here, we elucidate various biological properties of P20 and the involvement of a single domain in its activities. P20 displayed a strong self-interaction in vitro and in vivo, and cross-linking assays demonstrated its oligomerization. Domain mapping, using the bacterial two-hybrid system, indicated that the self-interacting domain overlaps the RNA-binding domain in the N-terminal arginine-rich motif (ARM) of P20. The deletion of the ARM abolished the self-interaction of P20 in vitro and in vivo and impaired its intracellular targeting and efficient cell-to-cell movement in N. benthamiana leaves. Moreover, RNA and protein accumulation of the ARM deletion mutant of satBaMV was significantly reduced in leaves systemically coinfected with Bamboo mosaic potexvirus and satBaMV. This is the first report of the involvement of ARM in various biological activities of a satellite RNA-encoded protein during infection of its host.


Additional keyword: protein-protein interaction .

© 2006 The American Phytopathological Society