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  The Structural Basis for the Suppression of RNA Silencing by a Plant Viral Protein
Copyright 2005 by Wayne Decatur. All rights reserved.

RNA silencing is a gene inactivation system in many eukaryotes that relies on tiny RNAs as the targeting molecules. One function of RNA silencing is to act in surveillance against molecular parasites, such as viruses. Double-stranded RNA triggers the RNA silencing pathway and most plant viruses use a double-stranded RNA to replicate their genome. Various plant viruses have developed evasion techniques to circumvent this surveillance sytem. In one such evasion strategy, the plant viral protein p19 suppresses a plants anti-viral RNA silencing response. p19 binds with high affinity double-stranded RNA silencing mediator, called siRNA, and this binding sequesters the siRNA, preventing its participation in later steps of RNA silencing. Structural studies have now revealed how p19 selectively recognizes the double-stranded siRNA.
Please click on a chapter to begin:

  1. Introduction to the RNA Silencing Suppressor p19 and its substrate.

  2. Basis for the selective recognition of siRNA by p19

I suggest you check out the references below and citations therein if you would like any more information about p19 or the phenomenon of RNA silencing, which is also known as RNA interference or RNAi.

  1. Vargason JM, Szittya G, Burgyan J, Tanaka Hall TM. 2003 Size selective recognition of siRNA by an RNA silencing suppressor. Cell. 115(7):799-811. [The pdb file, 1rpu, associated with this study is used in this PiPE.]
  2. Ye K, Malinina L, Patel DJ. 2003 Recognition of small interfering RNA by a viral suppressor of RNA silencing. Nature. 426(6968):874-878. Epub 2003 Dec 3.
  3. Evelyn Jabri. 2004. Sizing up small RNAs. Nature Structural & Molecular Biology 11: 112.
  4. Baulcombe DC, Molnar A. 2004. Crystal structure of p19--a universal suppressor of RNA silencing. Trends Biochem Sci. 29(6):279-281.
  5. Lingel A, Sattler M. 2005. Novel modes of protein-RNA recognition in the RNAi pathway. Curr Opin Struct Biol. 15(1):107-115.


This is a Presentation in Protein Explorer (PiPE) prepared with Development of Protein Explorer was supported by a grant to Eric Martz from the Division of Undergraduate Education of the US National Science Foundation.