Structural Basis for Processivity and Single-Strand Specificity of RNase II

Yuhong Zuo, Helen A. Vincent, Jianwei Zhang, Yong Wang, Murray P Deutscher, Arun Malhotra

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

RNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3′→5′ hydrolytic enzymes that play an important role in mRNA decay. Here, we report the crystal structure of E. coli RNase II, which reveals an architecture reminiscent of the RNA exosome. Three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single-stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3′ single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single-stranded RNA.

Original languageEnglish
Pages (from-to)149-156
Number of pages8
JournalMolecular Cell
Volume24
Issue number1
DOIs
StatePublished - Oct 6 2006

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RNA
Exosome Multienzyme Ribonuclease Complex
Exoribonucleases
RNA Stability
Hydrolysis
Escherichia coli
exoribonuclease II
Enzymes
Proteins
RNA-Binding Motifs

Keywords

  • RNA

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Structural Basis for Processivity and Single-Strand Specificity of RNase II. / Zuo, Yuhong; Vincent, Helen A.; Zhang, Jianwei; Wang, Yong; Deutscher, Murray P; Malhotra, Arun.

In: Molecular Cell, Vol. 24, No. 1, 06.10.2006, p. 149-156.

Research output: Contribution to journalArticle

Zuo, Yuhong ; Vincent, Helen A. ; Zhang, Jianwei ; Wang, Yong ; Deutscher, Murray P ; Malhotra, Arun. / Structural Basis for Processivity and Single-Strand Specificity of RNase II. In: Molecular Cell. 2006 ; Vol. 24, No. 1. pp. 149-156.
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