Structural basis for double-stranded RNA processing by Dicer

Ian J. MacRae, Kaihong Zhou, Fei Li, Adrian Repic, Angela N. Brooks, W. Zacheus Cande, Paul D. Adams, Jennifer A. Doudna

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)195-198
Number of pages4
JournalScience
Volume311
Issue number5758
DOIs
StatePublished - Jan 13 2006

ASJC Scopus subject areas

  • General

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