한국식물병리학회:학술대회논문집 (Proceedings of the Korean Society of Plant Pathology Conference)
- 한국식물병리학회 2003년도 정기총회 및 추계학술발표회
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- Pages.76.1-76
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- 2003
The coat protein of Turnip crinkle virus is required a full-length to maintain suppressing activity to RNA silencing but no relation with eliciting resistance by N-terminal region in Arabidopsis.
- Park, Chang-Won (Department of Biology 8t Medicinal Science, Pai Chai University) ;
- Feng Qu (School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska) ;
- Tao Ren (School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska) ;
- T. Jack Morris (School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska)
- 발행 : 2003.10.01
초록
The coat protein (CP) of Turnip crinkle virus (TCV) is organized into 3 distinct domains, R domain (RNA-binding) connected by an arm, 5 domain and P domain. We have previously shown that the CP of TCV strongly suppresses RNA silencing, and have mapped N-terminal R domain of which is also the elicitor of resistance response in the Arabidopsis ecotype Di-17 carrying the HRT resistance gene. In order to map the region in the TCV CP that is responsible for silencing suppression, a series of CP mutants were constructed, transformed into Agrobacterium, coinfiltrated either with HC-Pro (the helper component proteinase of tobacco etch potyvirus) known as a suppressor of PTGS or GFP constructs into leaves of Nicotiana benthmiana expressing GFP transgenically. In the presence of HC-Pro, all CP mutants were well protected, accumulating mutant CP mRNAs and their proteins even 5 days post-infiltration (DPI). In the presence of GFP, some mutant constructs which showed the accumulation of CP mutants and GFP mRNAs at early stage but eventually degraded at 5 DPI. Only a mutant which carrying 4 amino acid deletion of R domain was tolerable to maintain suppressing activity, suggesting that the suppressing activity is not directly related with the eliciting activity. A transient assay also revealed that the mutants synthesized their proteins, suggesting that a full length of CP sequences and its intact structure are required to stabilize CP, which suppresses the RNA silencing.
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