Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase

Frolova, Ludmila; Судомоина, М. А.; Grigorieva, Arina Yu.; Zinovieva, Olga L.; Kisselev, Lev L.

doi:10.1016/0378-1119(91)90624-k

Cited by 52 publications

(43 citation statements)

References 26 publications

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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%

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Cérini

Sémériva

Gratecos

1997

European Journal of Biochemistry

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In Drosophila, glutamyl‐prolyl‐tRNA synthetase is a multifunctional synthetase encoded by a unique gene and composed of three domains: the amino‐ and carboxy‐terminal domains catalyze the aminoacylation of glutamic acid and proline tRNA species, respectively, and the central domain is made of 75 amino acids repeated six times amongst which 46 are highly conserved and constitute the repeated motifs [Cerini, C., Kerjan, P., Astier, M., Gratecos, D., Mirande, M. & Sémériva, M. (1991) EMBO J. 10, 4267–4277]. The intron/exon organization of the Drosophila gene reveals the presence of six exons among which four are in the 5′‐end encoding glutamic acid activity. Only one exon encodes the repeated motifs. A comparison of introns positions, intron classes and intron/exon boundaries in the Drosophila gene and in its human counterpart is compatible with the intron‐early hypothesis presiding, at least in part, to the evolution of the synthetases. The full‐length fly protein is encoded by a 6.1‐kb mRNA which is expressed throughout development. In addition, a shorter transcript encompasses the 3′‐end of the cDNA and it is especially abundant in 5–10‐h embryos until the first larval stage. Expression of these two mRNAs seems to be controlled by two independent promoters. The 6.1‐kb mRNA promoter is probably localized in the 5′‐end of the gene. The small mRNA promoter resides in the 4th intron and evidence is provided that the mRNA encodes only the domain corresponding to prolyl‐tRNA synthetase and is functional in vivo. Finally, transgenic flies have been established by using constructs corresponding to the three domains of the protein. Overexpression of the repeated motifs leads to a sterility of the flies that suggests a role of these motifs in linking the multienzyme complex to an, as yet, unknown structure of the protein synthesis apparatus.

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confidence: 99%

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Cérini

Sémériva

Gratecos

1997

European Journal of Biochemistry

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“…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.…”

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confidence: 99%

“…Independently, it has been shown that the amino acid sequence of one of the proteins stimulated by interferon y in human amnion cell cultures (termed y2 protein) [17] or HeLa cells (termed IFP 53 protein) [18, 191, or induced by interferon a or y in human fibroblasts (termed 56Kay protein) [20] is virtually the same as that of hTrpRS [16]. Furthermore, this interferon-induced protein exhibits TrpRS activity.…”

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Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?

Frolova

Fleckner

Justesen

et al. 1993

European Journal of Biochemistry

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This close similarity between mammalian TrpRS and cloned RF is unexpected given the distinct functional properties of these proteins. Consequently, the question arises as to whether the mammalian TrpRS and RF activities reside on identical or very similar polypeptides. Alternatively, one may assume that the cloned rabbit cDNA encodes a protein other than rRF.Several properties (immunochemical, biochemical and physico-chemical) of mammalian TrpRS and RF have been compared. rTrpRS and rRF have distinct thermostability behaviours, and dissimilar chromatographic profiles on phosphocellulose. Both the anti-bTrpRS polyclonal antibodies and the monoclonal antibody Am2 strongly inhibit the bTrpRS and hTrpRS aminoacylation activities, but not the rRF activity. In addition, neither bTrpRS nor hTrpRS exhibit RF activity. It is concluded that (a) the functional centers responsible for the TrpRS and RF activities are structurally and functionally dissimilar and could hardly belong to the same protein domain; (b) RF and TrpRS probably reside on different polypeptide chains encoded by different genes, although it is still not excluded that the RF-and TrpRS-specific domains are situated on one and the same polypeptide chain; (c) the rabbit cDNA believed to encode RF, presumably encodes rTrpRS; this would explain why its deduced amino acid sequence has no similarity with bacterial RFs but is very similar to mammalian TrpRS.It has long been known that termination of translation is controlled by specific components of the protein-synthesizing machinery, including termination codons in the

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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%

Interferons induce accumulation of diadenosine triphosphate (Ap₃A) in human cultured cells

et al. 1996

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Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase

Cited by 52 publications

References 26 publications

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?

Interferons induce accumulation of diadenosine triphosphate (Ap₃A) in human cultured cells

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Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase

Cited by 52 publications

References 26 publications

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Evolution of The Aminoacyl‐tRNa Synthetase Family and The Organization of the Drosophila Glutamyl‐Prolyl‐tRNA Synthetase Gene — Intron/Exon Structure of the Gene, Control of Expression of the Two mRNAs, Selective Advantage of the Multienzyme Complex

Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?

Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells

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Interferons induce accumulation of diadenosine triphosphate (Ap₃A) in human cultured cells