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http://purl.uniprot.org/citations/31299085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31299085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31299085http://www.w3.org/2000/01/rdf-schema#comment"Translation is controlled by numerous accessory proteins and translation factors. In the yeast Saccharomyces cerevisiae, translation elongation requires an essential elongation factor, the ABCF ATPase eEF3. A closely related protein, New1, is encoded by a non-essential gene with cold sensitivity and ribosome assembly defect knock-out phenotypes. Since the exact molecular function of New1 is unknown, it is unclear if the ribosome assembly defect is direct, i.e. New1 is a bona fide assembly factor, or indirect, for instance due to a defect in protein synthesis. To investigate this, we employed yeast genetics, cryo-electron microscopy (cryo-EM) and ribosome profiling (Ribo-Seq) to interrogate the molecular function of New1. Overexpression of New1 rescues the inviability of a yeast strain lacking the otherwise strictly essential translation factor eEF3. The structure of the ATPase-deficient (EQ2) New1 mutant locked on the 80S ribosome reveals that New1 binds analogously to the ribosome as eEF3. Finally, Ribo-Seq analysis revealed that loss of New1 leads to ribosome queuing upstream of 3'-terminal lysine and arginine codons, including those genes encoding proteins of the cytoplasmic translational machinery. Our results suggest that New1 is a translation factor that fine-tunes the efficiency of translation termination or ribosome recycling."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkz600"xsd:string
http://purl.uniprot.org/citations/31299085http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkz600"xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Atkinson G.C."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Atkinson G.C."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Hauryliuk V."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Hauryliuk V."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Murina V."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Murina V."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Margus T."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Margus T."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Novacek J."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Novacek J."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Johansson M.J.O."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Johansson M.J.O."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Pochopien A.A."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Pochopien A.A."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Graf M."xsd:string
http://purl.uniprot.org/citations/31299085http://purl.uniprot.org/core/author"Graf M."xsd:string