“Our laboratory’s research focus is in the structural biology of post-transcriptional gene regulation.”

I think it is highly cited because the paper describes one of the first crystal structures of a protein with an siRNA and also because we demonstrated that double-stranded RNA could be recognized based on the length of the RNA rather than the sequence.

Because siRNA recognition by p19 is sequence independent, it suggests that p19 can be used to suppress RNAi in heterologous systems. Olivier Voinnet’s group at the Institut de Biologie Moléculaire des Plantes du CNRS has demonstrated that p19 can inhibit RNAi in HeLa cells (Plant Cell 16:1235-1250, 2004). We hope that p19 can be used to inhibit both siRNA and miRNA-directed RNA silencing.

Our laboratory’s research focus is in the structural biology of post-transcriptional gene regulation. It was a natural step for us to move toward studying proteins involved in RNAi. We are grateful to have established a wonderful collaboration with József Burgyán’s plant virology laboratory in Gödöllő, Hungary, to combine our mutual interests in this study.

RNA interference is a mechanism to turn genes off or silence them. This mechanism exists in both plants and animals. For plants, RNA interference acts as an immune system for the plant, protecting them from plant viruses. On the other hand, plant viruses have countered by developing proteins that will stop or slow RNA interference. One of these proteins is p19, the subject of our paper. Our collaborator had shown that p19 binds to small interfering RNAs, the molecules that direct which genes are silenced. This paper showed how the protein interacts with the RNAs and how they select for this specific type of small RNA.