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Area of Science:

  • Molecular Biology
  • Biochemistry
  • RNA Biology

Background:

  • Dicer is a ribonuclease crucial for RNA interference, processing double-stranded RNAs (dsRNAs) into small interfering RNAs (siRNAs).
  • Dicer possesses domains homologous to bacterial RNase III, an enzyme known to function as a homodimer.
  • Previous models proposed dsRNA interaction and cleavage by RNase III at two composite catalytic centers.

Purpose of the Study:

  • To investigate the catalytic mechanism of human Dicer and E. coli RNase III.
  • To determine the number of processing centers and the nature of RNA cleavage products.
  • To propose a functional model for Dicer's enzymatic activity.

Main Methods:

  • Site-directed mutagenesis of human Dicer and E. coli RNase III residues implicated in catalysis.
  • Analysis of the effect of mutations on RNA processing activity.
  • Integration of experimental data with structural information of RNase III.

Main Results:

  • Mutational analysis revealed that both Dicer and RNase III possess only one active processing center.
  • This single center contains two distinct RNA cleavage sites.
  • The enzymes generate RNA products with characteristic 2 nt 3' overhangs.

Conclusions:

  • Dicer likely functions through intramolecular dimerization of its two RNase III domains.
  • The PAZ and dsRBD domains assist in this intramolecular dimerization process.
  • The study clarifies the catalytic mechanism and quaternary structure of Dicer in RNA processing.