Noncatalytic assembly of ribonuclease III with double-stranded RNA

被引：111

作者：

Blaszczyk, J ^{[1
]}

Gan, JH ^{[1
]}

Tropea, JE ^{[1
]}

Court, DL ^{[1
]}

Waugh, DS ^{[1
]}

Ji, XH ^{[1
]}

机构：

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

来源：

STRUCTURE | 2004年 / 12卷 / 03期

关键词：

D O I：

10.1016/j.str.2004.02.004

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：

Ribonuclease III (RNase III) represents a family of double-stranded RNA (dsRNA) endonucleases. The simplest bacterial enzyme contains an endonuclease domain (endoND) and a dsRNA binding domain (dsRBD). RNase III can affect RNA structure and gene expression in either of two ways: as a dsRNA-processing enzyme that cleaves dsRNA, or as a dsRNA binding protein that binds but does not cleave dsRNA. We previously determined the endoND structure of Aquifex aeolicus RNase III (Aa-RNase III) and modeled a catalytic complex of full-length Aa-RNase III with dsRNA. Here, we present the crystal structure of Aa-RNase III in complex with dsRNA, revealing a noncatalytic assembly. The major differences between the two functional forms of RNase III(.)dsRNA are the conformation of the protein and the orientation and location of dsRNA. The flexibility of a 7 residue linker between the endoND and dsRBD enables the transition between these two forms.

引用

页码：457 / 466

页数：10

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[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].