Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes.
The nucleotide sequence of a cDNA coding human threonyl-tRNA synthetase has been determined. The predicted protein sequence is highly homologous to that of the yeast cytoplasmic, yeast mitochondria and Escherichia coli threonyl-tRNA synthetases. In particular, the three structural motifs recently shown to be common to class II aminoacyl-tRNA synthetases are present in the threonyl-tRNA synthetases from all sources. Primer extension and S1 nuclease analyses indicate that transcription initiates approximately 220-230 nucleotides upstream of the putative initiator methionine codon. This region contains a 10-nucleotide interrupted inverted repeat flanked by a 13-nucleotide interrupted direct repeat.
Cruzen
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Department of Biological Chemistry, College of Medicine, University of California, Irvine 92717.
Arfin
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D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology*; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012689:Sequence Homology, Nucleic Acid; D013914:Threonine-tRNA Ligase / Q000235:genetics*
D004247:DNA; D013914:Threonine-tRNA Ligase