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http://purl.uniprot.org/citations/11250908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11250908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11250908http://www.w3.org/2000/01/rdf-schema#comment"GCN2 stimulates translation of GCN4 mRNA in amino acid-starved cells by phosphorylating translation initiation factor 2. GCN2 is activated by binding of uncharged tRNA to a domain related to histidyl-tRNA synthetase (HisRS). The HisRS-like region contains two dimerization domains (HisRS-N and HisRS-C) required for GCN2 function in vivo but dispensable for dimerization by full-length GCN2. Residues corresponding to amino acids at the dimer interface of Escherichia coli HisRS were required for dimerization of recombinant HisRS-N and for tRNA binding by full-length GCN2, suggesting that HisRS-N dimerization promotes tRNA binding and kinase activation. HisRS-N also interacted with the protein kinase (PK) domain, and a deletion impairing this interaction destroyed GCN2 function without reducing tRNA binding; thus, HisRS-N-PK interaction appears to stimulate PK function. The C-terminal domain of GCN2 (C-term) interacted with the PK domain in a manner disrupted by an activating PK mutation (E803V). These results suggest that the C-term is an autoinhibitory domain, counteracted by tRNA binding. We conclude that multiple domain interactions, positive and negative, mediate the activation of GCN2 by uncharged tRNA."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.6.1425"xsd:string
http://purl.uniprot.org/citations/11250908http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.6.1425"xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Dong J."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Dong J."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Hu C."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Hu C."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Qiu H."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Qiu H."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Francklyn C.S."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Francklyn C.S."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Hinnebusch A.G."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/author"Hinnebusch A.G."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/pages"1425-1438"xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/pages"1425-1438"xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/title"The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/title"The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation."xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11250908http://purl.uniprot.org/core/volume"20"xsd:string