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

Gan, Jianhua ; Tropea, Joseph E ; Austin, Brian P ; Court, Donald L ; Waugh, David S ; Ji, Xinhua

Cell, 27 January 2006, Vol.124(2), pp.355-66 [Tạp chí có phản biện]

ISSN: 0092-8674 ; PMID: 16439209 Version:1

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  • Nhan đề:
    Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
  • Tác giả: Gan, Jianhua ; Tropea, Joseph E ; Austin, Brian P ; Court, Donald L ; Waugh, David S ; Ji, Xinhua
  • Chủ đề: RNA, Double-Stranded -- Chemistry ; Ribonuclease III -- Chemistry
  • Là 1 phần của: Cell, 27 January 2006, Vol.124(2), pp.355-66
  • Mô tả: 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...
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0092-8674 ; PMID: 16439209 Version:1

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