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Structural basis for double-stranded RNA processing by Dicer.

Ian J Macrae1, Kaihong Zhou, Fei Li

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

Science (New York, N.Y.)
|January 18, 2006
PubMed
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The Dicer enzyme acts as a molecular ruler, measuring double-stranded RNA (dsRNA) to precisely cut it into small fragments for RNA interference. Its structure ensures accurate cleavage at a specific distance from the dsRNA end.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • RNA interference (RNAi) is a crucial biological process for gene regulation.
  • Dicer is a key enzyme initiating RNAi by processing double-stranded RNA (dsRNA).

Purpose of the Study:

  • To elucidate the structural basis of Dicer's substrate recognition and cleavage mechanism.
  • To understand how Dicer precisely determines the length of small RNA fragments.

Main Methods:

  • X-ray crystallography was used to determine the structure of the intact Dicer enzyme.
  • Analysis of the spatial arrangement of Dicer's functional domains.

Main Results:

  • The PAZ domain, which binds dsRNA, is positioned relative to the RNase III catalytic domains.

Related Experiment Videos

  • A 65 angstrom distance was observed between the PAZ and RNase III domains, matching the length of 25 base pairs of dsRNA.
  • Dicer functions as a molecular ruler, measuring dsRNA length for accurate cleavage.

    • Conclusions:

    • Dicer's intrinsic structure dictates its function as a molecular ruler in dsRNA processing.
    • This structural feature ensures the generation of specific-sized small interfering RNAs (siRNAs) essential for RNAi.