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Crystal structure of p19--a universal suppressor of RNA silencing
David C Baulcombe1, Attila Molnár
1The Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich, NR4 7UH, UK. david.baucombe@sainsbury-laboratory.ac.uk
Abstract:
RNA silencing in plants has an antiviral role and, consequently, plant viruses encode counter-defensive suppressor proteins that block this process. The recently reported crystal structure of two Tombusvirus suppressor proteins reveals a novel RNA-binding structure and illustrates precisely how the silencing mechanism is blocked. These suppressor protein structures, combined with molecular analyses of their effects in animal and plant cells, are informative about RNA silencing mechanisms. They also suggest various ways that Tombusvirus suppressors can be used to investigate RNA silencing in plants and animals.
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