Abstract
Antibodies to Escherichia coli glycyl-tRNA synthetase (GlyRS) cross-react extensively with E. coli phenylalanyl-tRNA synthetase (PheRS). These data indicate that structural homology exists between these two enzymes, the only two aminoacyl-tRNA synthetases in E. coli having an α 2β 2 subunit structure. Although only limited similarities are found in the protein sequences deduced from their known gene sequences, the presence of common epitopes in GlyRS and PheRS adds to a rather long list of physical and chemical similarities between those proteins. In addition, antibodies directed at the α- and β-subunits of GlyRS inhibit both GlyRS and PheRS in the same relative manner, indicating that the function as well as the structure of subunits is similar in each enzyme. In contrast, GlyRS antibodies did not cross-react with a number of other aminoacyl-tRNA synthetase activities from E. coli, yeast, or Bacillus.
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