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http://purl.uniprot.org/citations/18469165http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18469165http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18469165http://www.w3.org/2000/01/rdf-schema#comment"The Smaug family of sequence-specific RNA binding proteins regulates mRNA translation and degradation by binding to consensus stem-loop structures in target mRNAs. Vts1p is a member of the Smaug protein family that regulates the stability of target transcripts in Saccharomyces cerevisiae. Here we focus on the mechanism of Vts1p-mediated mRNA decay. Using RNA reporters that recapitulate Vts1p-mediated decay in vivo, we demonstrate that Vts1p stimulates mRNA degradation through deadenylation mediated by the Ccr4p-Pop2p-Not deadenylase complex. We also show that Vts1p interacts with the Ccr4p-Pop2p-Not complex suggesting that Vts1p recruits the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs, resulting in transcript decay. Following deadenylation Vts1p target transcripts are decapped and subsequently degraded by the 5'-to-3' exonuclease Xrn1p. Decapping and 5'-to-3' decay is thought to occur in foci known as P-bodies, and we provide evidence that Vts1p function may involve P-bodies. Taken together with previous work, these data suggest that Smaug family members employ a conserved mechanism to induce transcript degradation that involves recruitment of the Ccr4-Pop2-Not deadenylase to target mRNAs."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.org/dc/terms/identifier"doi:10.1261/rna.955508"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.org/dc/terms/identifier"doi:10.1261/rna.955508"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Smibert C.A."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Smibert C.A."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Rendl L.M."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Rendl L.M."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Bieman M.A."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/author"Bieman M.A."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/name"RNA"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/name"RNA"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/pages"1328-1336"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/pages"1328-1336"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/title"S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/title"S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex."xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/18469165http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/18469165http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18469165
http://purl.uniprot.org/citations/18469165http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18469165
http://purl.uniprot.org/citations/18469165http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18469165
http://purl.uniprot.org/citations/18469165http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18469165