An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer

• Pierre Barraud ^[1] ; Stephan Emmerth ^[2] ; Yukiko Shimada ^[2] ; Hans-Rudolf Hotz ^[2] ; Frédéric H-T Allain ^[1] ; Marc Bühler ^[2]
  1. [1] Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland
  2. [2] Epigenetics, Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland; Universität Basel, Basel, Switzerland
• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 30, Nº. 20, 2011, págs. 4223-4235
• Idioma: inglés
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• Resumen

  • The Dicer ribonuclease Dcr1 plays an important role in the biogenesis of small regulatory RNAs. Surprisingly, RNA binding by the double-stranded RNA binding domain (dsRBD) is dispensable for Dcr1 function, while zinc coordination of the extended dsRBD is required for its nuclear localization and RNA silencing.