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rdf:type |
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lifeskim:mentions |
umls-concept:C0035668,
umls-concept:C0037791,
umls-concept:C0043393,
umls-concept:C0073240,
umls-concept:C0233820,
umls-concept:C0439855,
umls-concept:C0678594,
umls-concept:C1167622,
umls-concept:C1512046,
umls-concept:C1710236,
umls-concept:C1999230
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pubmed:issue |
7
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pubmed:dateCreated |
2011-7-11
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1878-4186
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
999-1010
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pubmed:meshHeading |
pubmed-meshheading:21742266-Base Sequence,
pubmed-meshheading:21742266-Binding Sites,
pubmed-meshheading:21742266-Blotting, Northern,
pubmed-meshheading:21742266-Models, Molecular,
pubmed-meshheading:21742266-Molecular Sequence Data,
pubmed-meshheading:21742266-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:21742266-Nucleic Acid Conformation,
pubmed-meshheading:21742266-Protein Binding,
pubmed-meshheading:21742266-Protein Conformation,
pubmed-meshheading:21742266-RNA, Double-Stranded,
pubmed-meshheading:21742266-RNA, Fungal,
pubmed-meshheading:21742266-RNA, Small Interfering,
pubmed-meshheading:21742266-Ribonuclease III,
pubmed-meshheading:21742266-Saccharomyces cerevisiae,
pubmed-meshheading:21742266-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:21742266-Substrate Specificity
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pubmed:year |
2011
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pubmed:articleTitle |
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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pubmed:affiliation |
Department of Chemistry and Biochemistry, P.O. Box 951569, University of California, Los Angeles, CA 90095-1569, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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