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Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA.
A 3.8 Kb DNA fragment, which contains the structural gene of aspartyl-tRNA synthetase (AspRS) and its flanking regions, has been fully sequenced by the combined M13/dideoxy chain terminator method. From the single open reading frame of correct length (1671 bp) we deduced an amino acid sequence consistent with that of several peptides of AspRS. No significant internal sequence repeats were observed in the primary structure of the protein. The AspRS gene (APS) has a codon usage pattern typical of non abundant proteins. S1 nuclease analysis of APS mRNA showed a major start 17 bases downstream from a "TATA box" and stops near an RNA polymerase terminator sequence.
PMID: 3513127 [PubMed - indexed for MEDLINE]
PMCID: PMC339550
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Cited by 10 PubMed Central articles
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A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding.
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[EMBO J. 2000]
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Molecular cloning, sequence, structural analysis and expression of the histidyl-tRNA synthetase gene from Streptococcus equisimilis.
Menguito CA, Keherly MJ, Tang C, Papaconstantinou J, Weigel PH.
Nucleic Acids Res. 1993 Feb 11; 21(3):615-20.
[Nucleic Acids Res. 1993]
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Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.
Eriani G, Cavarelli J, Martin F, Dirheimer G, Moras D, Gangloff J.
Proc Natl Acad Sci U S A. 1993 Nov 15; 90(22):10816-20.
[Proc Natl Acad Sci U S A. 1993]
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