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Characterization of the TRBP domain required for Dicer interaction and function in RNA interference |
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| Authors: | Sylvanne M Daniels Carlos E Melendez-Peña Robert J Scarborough Aïcha Daher Helen S Christensen Mohamed El Far Damian FJ Purcell Sébastien Lainé Anne Gatignol |
| Affiliation: | 1. Virus-Cell Interactions Laboratory, Lady Davis Institute for Medical Research, 3999 C?te Ste Catherine, Montréal, Québec, H3T1E2, Canada 2. Department of Microbiology and Immunology, McGill University, Montréal, Québec, Canada 5. Current address: GSK-Biological, Laval, QC, Canada 4. Department of Microbiology and Immunology, University of Melbourne, Parkville, Australia 6. Current address: Centre de Recherche du CHUM, H?pital Saint-Luc, Montréal, QC, Canada 7. Current address: CNRS UMR, 5097, Université de Bordeaux 2, Bordeaux, France 3. Department of Experimental Medicine, McGill University, Montréal, Québec, Canada |
| Abstract: | BackgroundDicer, Ago2 and TRBP are the minimum components of the human RNA-induced silencing complex (RISC). While Dicer and Ago2 are RNases, TRBP is the double-stranded RNA binding protein (dsRBP) that loads small interfering RNA into the RISC. TRBP binds directly to Dicer through its C-terminal domain. |
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