Structural Basis for Double-Stranded RNA Processing by Dicer-Reference-Cited by-同舟云学术

Structural Basis for Double-Stranded RNA Processing by Dicer

Published:2006-01-13 Issue:5758 Volume:311 Page:195-198
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

MacRae Ian J.¹²³⁴,Zhou Kaihong¹²³⁴,Li Fei¹²³⁴,Repic Adrian¹²³⁴,Brooks Angela N.¹²³⁴,Cande W. Zacheus¹²³⁴,Adams Paul D.¹²³⁴,Doudna Jennifer A.¹²³⁴

Affiliation:

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

2. Department of Chemistry, University of California, Berkeley, CA 94720, USA.

3. Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.

4. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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