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

被引：187

作者：

Gan, JH ^{[1
]}

Tropea, JE ^{[1
]}

Austin, BP ^{[1
]}

Court, DL ^{[1
]}

Waugh, DS ^{[1
]}

Ji, XH ^{[1
]}

机构：

[1] NCI, Canc Res Ctr, NIH, Ft Detrick, MD 21702 USA

来源：

CELL | 2006年 / 124卷 / 02期

关键词：

D O I：

10.1016/j.cell.2005.11.034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：355 / 366

页数：12

共 54 条

[1] Structure of the nuclease domain of ribonuclease III from M-tuberculosis at 2.1 Å [J].