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J. Biol. Chem., Vol. 266, Issue 15, 9919-9923, 05, 1991

Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes

ME Cruzen and SM Arfin
Department of Biological Chemistry, College of Medicine, University of California, Irvine 92717.

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.
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