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Structural basis for double-stranded RNA processing by Dicer.

Authors
  • Ij, Macrae
  • K, Zhou
  • F, Li
  • A, Repic
  • Angela Brooks
  • Wz, Cande
  • Pd, Adams
  • Ja, Doudna
Type
Published Article
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Volume
311
Issue
5758
Pages
195–198
Source
UCSC Bioinformatics biomedical-ucsc
License
Unknown

Abstract

The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.

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