Abstract
THE carcinogenic and mutagenic compound, 4-nitroquinoline 1-oxide (4NQO) and its reduced metabolite, 4-hydroxyaminoquinoline 1-oxide (4HAQO) bind covalently to cellular macromolecules such as nucleic acid and protein1–7. As 4HAQO rarely binds to nucleic acid in buffer solutions, it was suggested that a metabolic activation of 4HAQO is involved in the in vivo reaction. The presence of an activating enzyme has been demonstrated in extracts of rat ascites hepatoma cells and baker' yeast8,9. The enzyme activates 4HAQO to bind to nuclei acid or protein in the presence of ATP, L-serine and Mg2+ (ref.9). The nucleic acid adducts formed in the enzyme system show essentially the same chromatographic patterns as purine adducts formed in vivo4,6,8. Moreover, the DNA lesions caused by 4HAQO binding in the in vitro enzyme system like those lesions formed in vivo, can be repaired by the excision repair mechanism in Bacillus subtilis10. We have now purified oating 4HAQO-activating enzyme from bakers' yeast and report here that this enzyme is seryl-tRNA synthetase.
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TADA, M., TADA, M. Seryl-tRNA synthetase and activation of the carcinogen 4-nitroquinoline 1-oxide. Nature 255, 510–512 (1975). https://doi.org/10.1038/255510a0
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DOI: https://doi.org/10.1038/255510a0
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