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    Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing

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    Authors
    Ansel, K. Mark
    Pastor, William A.
    Rath, Nicola
    Lapan, Ariya D.
    Glasmacher, Elke
    Wolf, Christine
    Smith, Laura C.
    Papadopoulou, Nikoletta
    Lamperti, Edward D.
    Tahiliani, Mamta
    Ellwart, Joachim W.
    Shi, Yujiang
    Kremmer, Elisabeth
    Rao, Anjana
    Heissmeyer, Vigo
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    UMass Chan Affiliations
    Immune Disease Institute
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2008-04-29
    Keywords
    Animals; Exonucleases; Mice; Mice, Knockout; RNA Interference; *RNA Processing, Post-Transcriptional; RNA, Ribosomal; RNA, Ribosomal, 5.8S; Ribosomes
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1038/nsmb.1417
    Abstract
    Eri1 is a 3'-to-5' exoribonuclease conserved from fission yeast to humans. Here we show that Eri1 associates with ribosomes and ribosomal RNA (rRNA). Ribosomes from Eri1-deficient mice contain 5.8S rRNA that is aberrantly extended at its 3' end, and Eri1, but not a catalytically inactive mutant, converts this abnormal 5.8S rRNA to the wild-type form in vitro and in cells. In human and murine cells, Eri1 localizes to the cytoplasm and nucleus, with enrichment in the nucleolus, the site of preribosome biogenesis. RNA binding residues in the Eri1 SAP and linker domains promote stable association with rRNA and thereby facilitate 5.8S rRNA 3' end processing. Taken together, our findings indicate that Eri1 catalyzes the final trimming step in 5.8S rRNA processing, functionally and spatially connecting this regulator of RNAi with the basal translation machinery.
    Source
    Nat Struct Mol Biol. 2008 May;15(5):523-30. Epub 2008 Apr 27. Link to article on publisher's site
    DOI
    10.1038/nsmb.1417
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32940
    PubMed ID
    18438418
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1038/nsmb.1417
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