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    Yeast Upf1 CH domain interacts with Rps26 of the 40S ribosomal subunit

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    Authors
    Min, Ei Ei
    Roy, Bijoyita
    Amrani, Nadia
    He, Feng
    Jacobson, Allan
    UMass Chan Affiliations
    Department of Microbiology and Physiological Systems
    Document Type
    Journal Article
    Publication Date
    2013-08-01
    Keywords
    Adenosine Triphosphatases
    Codon, Nonsense
    Models, Molecular
    Mutagenesis, Site-Directed
    Nonsense Mediated mRNA Decay
    Protein Interaction Domains and Motifs
    Protein Subunits
    RNA Helicases
    RNA, Fungal
    Ribosomal Proteins
    Saccharomyces cerevisiae
    Saccharomyces cerevisiae Proteins
    NMD
    RNA helicase
    ribosomal proteins
    Amino Acids, Peptides, and Proteins
    Biochemistry
    Fungi
    Nucleic Acids, Nucleotides, and Nucleosides
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    Link to Full Text
    http://dx.doi.org/10.1261/rna.039396.113
    Abstract
    The central nonsense-mediated mRNA decay (NMD) regulator, Upf1, selectively targets nonsense-containing mRNAs for rapid degradation. In yeast, Upf1 preferentially associates with mRNAs that are NMD substrates, but the mechanism of its selective retention on these mRNAs has yet to be elucidated. Previously, we demonstrated that Upf1 associates with 40S ribosomal subunits. Here, we define more precisely the nature of this association using conventional and affinity-based purification of ribosomal subunits, and a two-hybrid screen to identify Upf1-interacting ribosomal proteins. Upf1 coimmunoprecipitates specifically with epitope-tagged 40S ribosomal subunits, and Upf1 association with high-salt washed or puromycin-released 40S subunits was found to occur without simultaneous eRF1, eRF3, Upf2, or Upf3 association. Two-hybrid analyses and in vitro binding assays identified a specific interaction between Upf1 and Rps26. Using mutations in domains of UPF1 known to be crucial for its function, we found that Upf1:40S association is modulated by ATP, and Upf1:Rps26 interaction is dependent on the N-terminal Upf1 CH domain. The specific association of Upf1 with the 40S subunit is consistent with the notion that this RNA helicase not only triggers rapid decay of nonsense-containing mRNAs, but may also have an important role in dissociation of the premature termination complex.
    Source

    Min EE, Roy B, Amrani N, He F, Jacobson A. Yeast Upf1 CH domain interacts with Rps26 of the 40S ribosomal subunit. RNA. 2013 Aug;19(8):1105-15. doi:10.1261/rna.039396.113. Link to article on publisher's site

    DOI
    10.1261/rna.039396.113
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/30146
    PubMed ID
    23801788
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    ae974a485f413a2113503eed53cd6c53
    10.1261/rna.039396.113
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