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http://purl.uniprot.org/citations/30911188http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30911188http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30911188http://www.w3.org/2000/01/rdf-schema#comment"Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved 5'-to-3' exoribonuclease Xrn1 has a crucial role in eukaryotic mRNA homeostasis by degrading decapped or cleaved mRNAs post-translationally and, more surprisingly, also co-translationally. Here we report that active Xrn1 can directly and specifically interact with the translation machinery. A cryo-electron microscopy structure of a programmed Saccharomyces cerevisiae 80S ribosome-Xrn1 nuclease complex reveals how the conserved core of Xrn1 enables binding at the mRNA exit site of the ribosome. This interface provides a conduit for channelling of the mRNA from the ribosomal decoding site directly into the active center of the nuclease, thus separating mRNA decoding from degradation by only 17 ± 1 nucleotides. These findings explain how rapid 5'-to-3' mRNA degradation is coupled efficiently to its final round of mRNA translation."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.org/dc/terms/identifier"doi:10.1038/s41594-019-0202-5"xsd:string
http://purl.uniprot.org/citations/30911188http://purl.org/dc/terms/identifier"doi:10.1038/s41594-019-0202-5"xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Cheng J."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Cheng J."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Buschauer R."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Buschauer R."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Jacquier A."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Jacquier A."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Becker T."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Becker T."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Beckmann R."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Beckmann R."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Berninghausen O."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Berninghausen O."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Beatrix B."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Beatrix B."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Fromont-Racine M."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Fromont-Racine M."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Tesina P."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Tesina P."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Kater L."xsd:string
http://purl.uniprot.org/citations/30911188http://purl.uniprot.org/core/author"Kater L."xsd:string