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    Argonaute protein identity and pairing geometry determine cooperativity in mammalian RNA silencing

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    Authors
    Broderick, Jennifer A.
    Salomon, William E.
    Ryder, Sean P.
    Aronin, Neil
    Zamore, Phillip D.
    Student Authors
    Jennifer A. Broderick
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2011-10-01
    Keywords
    Animals; Base Sequence; Cells, Cultured; Eukaryotic Initiation Factors; Humans; Mice; Protein Binding; *RNA Interference; RNA, Small Interfering
    Biochemistry, Biophysics, and Structural Biology
    Life Sciences
    Medicine and Health Sciences
    Neuroscience and Neurobiology
    
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    Abstract
    Small RNAs loaded into Argonaute proteins direct silencing of complementary target mRNAs. It has been proposed that multiple, imperfectly complementary small interfering RNAs or microRNAs, when bound to the 3' untranslated region of a target mRNA, function cooperatively to silence target expression. We report that, in cultured human HeLa cells and mouse embryonic fibroblasts, Argonaute1 (Ago1), Ago3, and Ago4 act cooperatively to silence both perfectly and partially complementary target RNAs bearing multiple small RNA-binding sites. Our data suggest that for Ago1, Ago3, and Ago4, multiple, adjacent small RNA-binding sites facilitate cooperative interactions that stabilize Argonaute binding. In contrast, small RNAs bound to Ago2 and pairing perfectly to an mRNA target act independently to silence expression. Noncooperative silencing by Ago2 does not require the endoribonuclease activity of the protein: A mutant Ago2 that cannot cleave its mRNA target also silences noncooperatively. We propose that Ago2 binds its targets by a mechanism fundamentally distinct from that used by the three other mammalian Argonaute proteins.
    Source
    RNA. 2011 Oct;17(10):1858-69. Epub 2011 Aug 30. Link to article on publisher's site
    DOI
    10.1261/rna.2778911
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33232
    PubMed ID
    21878547
    Related Resources
    Link to Article in PubMed
    Rights
    Copyright © 2011 RNA Society. Freely available online through the RNA Open Access option.
    ae974a485f413a2113503eed53cd6c53
    10.1261/rna.2778911
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    Morningside Graduate School of Biomedical Sciences Scholarly Publications

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