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http://purl.uniprot.org/citations/37595043http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37595043http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37595043http://www.w3.org/2000/01/rdf-schema#comment"Pseudouridine is enriched in ribosomal, spliceosomal, transfer, and messenger RNA and thus integral to the central dogma. The chemical basis for how pseudouridine affects the molecular apparatus such as ribosome, however, remains elusive owing to the lack of structures without this natural modification. Here, we studied the translation of a hypopseudouridylated ribosome initiated by the internal ribosome entry site (IRES) elements. We analyzed eight cryo-electron microscopy structures of the ribosome bound with the Taura syndrome virus IRES in multiple functional states. We found widespread loss of pseudouridine-mediated interactions through water and long-range base pairings. In the presence of the translocase, eukaryotic elongation factor 2, and guanosine 5'-triphosphate hydrolysis, the hypopseudouridylated ribosome favors a rare unconducive conformation for decoding that is partially recouped in the ribosome population that remains modified at the P-site uridine. The structural principles learned establish the link between functional defects and modification loss and are likely applicable to other pseudouridine-associated processes."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.adg8190"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.adg8190"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Rai J."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/author"Rai J."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/name"Sci. Adv."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/name"Sci Adv"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/pages"eadg8190"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/pages"eadg8190"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/title"Regulation of translation by ribosomal RNA pseudouridylation."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/title"Regulation of translation by ribosomal RNA pseudouridylation."xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/37595043http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/37595043http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37595043
http://purl.uniprot.org/citations/37595043http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37595043
http://purl.uniprot.org/citations/37595043http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37595043
http://purl.uniprot.org/citations/37595043http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37595043