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. 2006 Jan 13;311(5758):195-8.
doi: 10.1126/science.1121638.

Structural basis for double-stranded RNA processing by Dicer

Ian J Macrae  1 , Kaihong Zhou, Fei Li, Adrian Repic, Angela N Brooks, W Zacheus Cande, Paul D Adams, Jennifer A Doudna
Affiliations

Structural basis for double-stranded RNA processing by Dicer

Ian J Macrae et al. Science. .

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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