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http://purl.uniprot.org/citations/11101534http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11101534http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11101534http://www.w3.org/2000/01/rdf-schema#comment"GCN2 stimulates GCN4 translation in amino acid-starved cells by phosphorylating the alpha-subunit of translation initiation factor 2. GCN2 function in vivo requires the GCN1/GCN20 complex, which binds to the N-terminal domain of GCN2. A C-terminal segment of GCN1 (residues 2052-2428) was found to be necessary and sufficient for binding GCN2 in vivo and in vitro. Overexpression of this fragment in wild-type cells impaired association of GCN2 with native GCN1 and had a dominant Gcn(-) phenotype, dependent on Arg2259 in the GCN1 fragment. Substitution of Arg2259 with Ala in full-length GCN1 abolished complex formation with native GCN2 and destroyed GCN1 regulatory function. Consistently, the Gcn(-) phenotype of gcn1-R2259A, but not that of gcn1Delta, was suppressed by overexpressing GCN2. These findings prove that GCN2 binding to the C-terminal domain of GCN1, dependent on Arg2259, is required for high level GCN2 function in vivo. GCN1 expression conferred sensitivity to paromomycin in a manner dependent on its ribosome binding domain, supporting the idea that GCN1 binds near the ribosomal acceptor site to promote GCN2 activation by uncharged tRNA."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.23.6622"xsd:string
http://purl.uniprot.org/citations/11101534http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.23.6622"xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/author"Hinnebusch A.G."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/author"Hinnebusch A.G."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/author"Sattlegger E."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/author"Sattlegger E."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/pages"6622-6633"xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/pages"6622-6633"xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/title"Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/title"Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells."xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/11101534http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/11101534http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11101534
http://purl.uniprot.org/citations/11101534http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11101534
http://purl.uniprot.org/citations/11101534http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11101534
http://purl.uniprot.org/citations/11101534http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11101534
http://purl.uniprot.org/uniprot/P33892http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11101534
http://purl.uniprot.org/uniprot/P15442http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11101534