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 language | English (US) |
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Pages (from-to) | 195-198 |
Number of pages | 4 |
Journal | Science |
Volume | 311 |
Issue number | 5758 |
DOIs | |
State | Published - Jan 13 2006 |
ASJC Scopus subject areas
- General