1991
DOI: 10.1016/0378-1119(91)90624-k
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Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase

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Cited by 52 publications
(43 citation statements)
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“…The repeated units present in the core domains of the chimeric glutamyl-prolyl-tRNA synthetase (GluPro-RS) display structural features optimally suited to serve as a template for the association of the other components to the multienzyme complex. A single copy of the repeated motif exists in the N-terminal position of Trp-tRNA and His-tRNA synthetases which are proteins that never associate in the complexes (Tsui and Siminovitch, 1987;Frolova et al, 1991;Timchenko and Caskey, 1994). In fact, amino acid substitutions in the consensus sequence of these single-copy motifs suggest that they cannot play the same role as in the complex (Cerini et al, 1991).…”
mentioning
confidence: 99%
“…The repeated units present in the core domains of the chimeric glutamyl-prolyl-tRNA synthetase (GluPro-RS) display structural features optimally suited to serve as a template for the association of the other components to the multienzyme complex. A single copy of the repeated motif exists in the N-terminal position of Trp-tRNA and His-tRNA synthetases which are proteins that never associate in the complexes (Tsui and Siminovitch, 1987;Frolova et al, 1991;Timchenko and Caskey, 1994). In fact, amino acid substitutions in the consensus sequence of these single-copy motifs suggest that they cannot play the same role as in the complex (Cerini et al, 1991).…”
mentioning
confidence: 99%
“…C pairs (CGGGCAGGGGCCC ; nucleotides 634 -646), and therefore is strongly compressed during sequencing gel electrophoresis. This may lead to errors: indeed, it suffices to add one C residue in this region (at the level of nucleotides 644-646) and to omit one A residue downstream (at the level of nucleotide 663 or 664) of the sequence to preserve the open reading frame and to generate the same sequence as in bTrpRS and hTrpRS [16,17]. Furthermore, the deduced amino acid sequence of purified rRF was not confirmed by peptide sequencing of pure rRF preparations as has been done for bTrpRS [15].…”
Section: Comparison Of Mammalian Trprs and Rf And Their Activitiesmentioning
confidence: 99%
“…Asterisks denote identical residues with hTrpRS. ' h o adjacent amino acids in hTrpRS, Ser213 and 51-214, indicated above the hTrpRS sequence, reflect differences in nucleotide sequence between two hTrpRS cDNA clones [16]. The putative ATP (HVGH) and tRNA (KMSAS) binding sites in hTrpRS are underlined.…”
mentioning
confidence: 99%
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“…One of the genes stimulated by IFNs is a tryptophanyltRNA synthetase (TrpRS, EC 6.1.1.2), the enzyme involved in protein synthesis [6]. The amino acid sequence and the exonintron organisation of the TrpRS gene are known [7,8]. The gene contains in the 5'-regulatory region the ISRE and GAS elements [8] and TrpRS is induced by IFNs ct and 7 in cultured cells [9 11].…”
Section: Introductionmentioning
confidence: 99%