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Science. 2006 Jan 13;311(5758):195-8.

Structural basis for double-stranded RNA processing by Dicer.

Author information

1
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

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.

PMID:
16410517
DOI:
10.1126/science.1121638
[Indexed for MEDLINE]
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