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http://purl.uniprot.org/citations/20566627http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20566627http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20566627http://www.w3.org/2000/01/rdf-schema#comment"During translation, aminoacyl-tRNAs are delivered to the ribosome by specialized GTPases called translation factors. Here, we report the tRNA binding to the P-site of 40 S ribosomes by a novel GTP-independent factor eIF2D isolated from mammalian cells. The binding of tRNA(i)(Met) occurs after the AUG codon finds its position in the P-site of 40 S ribosomes, the situation that takes place during initiation complex formation on the hepatitis C virus internal ribosome entry site or on some other specific RNAs (leaderless mRNA and A-rich mRNAs with relaxed scanning dependence). Its activity in tRNA binding with 40 S subunits does not require the presence of the aminoacyl moiety. Moreover, the factor possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40 S subunit. The corresponding gene is found in all eukaryotes and includes an SUI1 domain present also in translation initiation factor eIF1. The versatility of translation initiation strategies in eukaryotes is discussed."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.119693"xsd:string
http://purl.uniprot.org/citations/20566627http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.119693"xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Shatsky I.N."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Shatsky I.N."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Merrick W.C."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Merrick W.C."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Andreev D.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Andreev D.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Dmitriev S.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Dmitriev S.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Dunaevsky J.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Dunaevsky J.E."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Ivanov P.A."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Ivanov P.A."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Terenin I.M."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/author"Terenin I.M."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/pages"26779-26787"xsd:string
http://purl.uniprot.org/citations/20566627http://purl.uniprot.org/core/pages"26779-26787"xsd:string