Abstract
A covalent adduct of an aminoacyl tRNA synthetase and uracil nucleoside has been isolated. The enzyme adduct is catalytically inactive; one nucleoside is bound per catalytic site. The release of uridine restores enzyme activity. The nucleoside attaches to a protein segment required for tRNA interaction. The findings add support to concepts of a covalent component for some protein–nucleic acid complexes.
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Starzyk, R., Koontz, S. & Schimmel, P. A covalent adduct between the uracil ring and the active site of an aminoacyl tRNA synthetase. Nature 298, 136–140 (1982). https://doi.org/10.1038/298136a0
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DOI: https://doi.org/10.1038/298136a0
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