NDLI: Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.

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Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.

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Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Zhonghua Hartman, Elon Roy, Kevin Chanfreau, Guillaume Feigon, Juli
Description	Country affiliation: United States Author Affiliation: Wang Z ( Department of Chemistry and Biochemistry, P.O. Box 951569, University of California, Los Angeles, CA 90095-1569, USA.)
Abstract	dsRBDs often bind dsRNAs with some specificity, yet the basis for this is poorly understood. Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its dsRBD to recognize a conserved tetraloop fold. However, the identification of a Rnt1p substrate with an AAGU tetraloop raised the question of whether Rnt1p binds to this noncanonical substrate differently than to A/uGNN tetraloops. The solution structure of Rnt1p dsRBD bound to an AAGU-capped hairpin reveals that the tetraloop undergoes a structural rearrangement upon binding to Rnt1p dsRBD to adopt a backbone conformation that is essentially the same as the AGAA tetraloop, and indicates that a conserved recognition mode is used for all Rnt1p substrates. Comparison of free and RNA-bound Rnt1p dsRBD reveals that tetraloop-specific binding requires a conformational change in helix 1. Our findings provide a unified model of binding site selection by this dsRBD.
File Format	HTM / HTML
ISSN	09692126
e-ISSN	18784186
DOI	10.1016/j.str.2011.03.022
Journal	Structure
Issue Number	7
Volume Number	19
Language	English
Publisher	Elsevier
Publisher Date	2011-07-13
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Rna, Double-stranded Metabolism Rna, Fungal Rna, Small Interfering Ribonuclease Iii Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Binding Sites Blotting, Northern Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Nucleic Acid Conformation Protein Binding Protein Conformation Chemistry Genetics Substrate Specificity Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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Structure of a yeast RNase III dsRBD complex with a non-canonical RNA substrate provides new insights into binding specificity of dsRBDs

Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.

Ribonuclease III mechanisms of double-stranded RNA cleavage.

Recognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III.

Ribonuclease III Processing of Coaxially Stacked RNA Helices

A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription.

Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiae.

Molecular biology. Rejoice--RNAi for yeast.

Yeast RNase P: catalytic activity and substrate binding are separate functions.

Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.

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Structure of a yeast RNase III dsRBD complex with a non-canonical RNA substrate provides new insights into binding specificity of dsRBDs

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Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.