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http://purl.uniprot.org/citations/19556969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19556969http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19556969http://www.w3.org/2000/01/rdf-schema#comment"Nonsense-mediated decay (NMD) is a eukaryotic quality control mechanism that degrades mRNAs carrying premature stop codons. In mammalian cells, NMD is triggered when UPF2 bound to UPF3 on a downstream exon junction complex interacts with UPF1 bound to a stalled ribosome. We report structural studies on the interaction between the C-terminal region of UPF2 and intact UPF1. Crystal structures, confirmed by EM and SAXS, show that the UPF1 CH-domain is docked onto its helicase domain in a fixed configuration. The C-terminal region of UPF2 is natively unfolded but binds through separated alpha-helical and beta-hairpin elements to the UPF1 CH-domain. The alpha-helical region binds sixfold more weakly than the beta-hairpin, whereas the combined elements bind 80-fold more tightly. Cellular assays show that NMD is severely affected by mutations disrupting the beta-hairpin binding, but not by those only affecting alpha-helix binding. We propose that the bipartite mode of UPF2 binding to UPF1 brings the ribosome and the EJC in close proximity by forming a tight complex after an initial weak encounter with either element."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2009.175"xsd:string
http://purl.uniprot.org/citations/19556969http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2009.175"xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Sattler M."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Sattler M."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Cusack S."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Cusack S."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Kadlec J."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Kadlec J."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Gutsche I."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Gutsche I."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Clerici M."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Clerici M."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Gehring N.H."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Gehring N.H."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Mourao A."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Mourao A."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Kulozik A."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/author"Kulozik A."xsd:string
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19556969http://purl.uniprot.org/core/date"2009"xsd:gYear