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http://purl.uniprot.org/citations/2129559http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2129559http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2129559http://www.w3.org/2000/01/rdf-schema#comment"By screening of an Escherichia coli plasmidic library using antibodies against aspartyl-tRNA synthetase (AspRS) several clones were obtained containing aspS, the gene coding for AspRS. We report here the nucleotide sequence of aspS and the corresponding primary structure of the aspartyl-tRNA synthetase, a protein of 590 amino acid residues with a Mr 65,913, a value in close agreement with that observed for the purified protein. Primer extension analysis of the aspS mRNA using reverse transcriptase located its 5'-end at 94 nucleotides upstream of the translation initiation AUG; nuclease S1 analysis located the 3'-end at 126 nucleotides downstream of the stop codon UGA. Comparison of the DNA-derived protein sequence with known aminoacyl-tRNA sequences revealed important homologies with asparaginyl- and lysyl-tRNA synthetases from E.coli; more than 25% of their amino acid residues are identical, the homologies being distributed preferencially in the first part and the carboxy-terminal end of the molecule. Mutagenesis directed towards a consensus tetrapeptide (Gly-Leu-Asp-Arg) and the carboxy-terminal end showed that both domains could be implicated in catalysis as well as in ATP binding."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.org/dc/terms/identifier"doi:10.1093/nar/18.23.7109"xsd:string
http://purl.uniprot.org/citations/2129559http://purl.org/dc/terms/identifier"doi:10.1093/nar/18.23.7109"xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Eriani G."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Eriani G."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Gangloff J."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Gangloff J."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Dirheimer G."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/author"Dirheimer G."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/pages"7109-7118"xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/pages"7109-7118"xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/title"Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/title"Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases."xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/2129559http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/2129559http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2129559
http://purl.uniprot.org/citations/2129559http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2129559
http://purl.uniprot.org/citations/2129559http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2129559
http://purl.uniprot.org/citations/2129559http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2129559