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Related Experiment Videos

A stepwise model for double-stranded RNA processing by ribonuclease III.

Jianhua Gan1, Gary Shaw, Joseph E Tropea

  • 1Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.

Molecular Microbiology
|December 1, 2007
PubMed
Summary
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Bacterial ribonuclease III (RNase III) uses two catalytic sites and two magnesium ions to cleave RNA. Crystal structures reveal how protein-RNA interactions and conformational changes enable this precise phosphoryl transfer reaction.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • RNA interference relies on small interfering RNAs generated by the ribonuclease III (RNase III) enzyme family.
  • Bacterial RNase III serves as a model system for understanding the mechanisms of this enzyme family.
  • Previous work demonstrated RNase III's dual catalytic sites for producing 2-nucleotide 3' overhangs.

Purpose of the Study:

  • To elucidate the structural and mechanistic basis of RNase III's catalytic activity.
  • To investigate the role of magnesium ions in RNase III function.
  • To model the catalytic complex and transition state of the RNase III reaction.

Main Methods:

  • X-ray crystallography of RNase III in complex with double-stranded RNA.
  • Biochemical assays to study enzymatic activity.

Related Experiment Videos

  • Computational modeling of protein-RNA complexes and transition states.

    • Main Results:

    • Three crystal structures reveal Mg(2+) essentiality for a catalytically competent complex.
    • The structures demonstrate how two Mg(2+) ions facilitate phosphodiester bond hydrolysis.
    • Conformational changes in both RNase III and its RNA substrate are critical for catalysis.
    • Models of the substrate-bound and transition-state complexes were generated.

    Conclusions:

    • RNase III employs a stepwise mechanism for phosphoryl transfer.
    • Structural insights explain the precise cleavage and 2-nt 3' overhang formation.
    • This study provides a detailed mechanistic understanding of RNase III function.