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Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III

  1. Author:
    Gan, J. H.
    Tropea, J. E.
    Austin, B. P.
    Court, D. L.
    Waugh, D. S.
    Ji, X. H.

  2. Author Address

    NCI, Canc Res Ctr, NIH, Ft Detrick, MD 21702 USA Ji, XH, NCI, Canc Res Ctr, NIH, Ft Detrick, MD 21702 USA
    1. Year: 2006
    2. Date: JAN 27
  2. Journal: Cell
    1. 124
    2. 2
    3. Pages: 355-366
  4. Type of Article: Article
  1. Abstract:

    Members of the ribonuclease III (RNase III) family are double-stranded RNA (dsRNA) specific endoribonucleases characterized by a signature motif in their active centers and a two-base 3' overhang in their products. While Dicer, which produces small interfering RNAs, is currently the focus of intense interest, the structurally simpler bacterial RNase III serves as a paradigm for the entire family. Here, we present the crystal structure of an RNase III-product complex, the first catalytic complex observed for the family. A 7 residue linker within the protein facilitates induced fit in protein-RNA recognition. A pattern of protein-RNA interactions, defined by four RNA binding motifs in RNase III and three protein-interacting boxes in dsRNA, is responsible for substrate specificity, while conserved amino acid residues and divalent cations are responsible for scissile-bond cleavage. The structure reveals a wealth of information about the mechanism of RNA hydrolysis that can be extrapolated to other RNase III family members

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External Sources

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  2. DOI: 10.1016/j.cell.2005.11.034
  3. View record in Web of Science®
  4. WOS: 000235068500023

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