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

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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

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Cite this

MacRae, I. J., Zhou, K., Li, F., Repic, A., Brooks, A. N., Cande, W. Z., Adams, P. D., & Doudna, J. A. (2006). Structural basis for double-stranded RNA processing by Dicer. Science, 311(5758), 195-198. https://doi.org/10.1126/science.1121638