A covalent adduct between the uracil ring and the active site of an aminoacyl tRNA synthetase

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 interact...

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Bibliographic Details
Published in:Nature (London) 1982-07, Vol.298 (5870), p.136-140
Main Authors: Starzyk, Ruth M, Koontz, Stephen W, Schimmel, Paul
Format: Article
Language:English
Subjects:
5-bromouridine
Alanine-tRNA Ligase - metabolism
alanyl-tRNA synthetase
Amino Acyl-tRNA Synthetases - metabolism
Binding Sites
Escherichia coli
Escherichia coli - enzymology
Kinetics
Protein Binding
RNA, Transfer - metabolism
Uracil
Uridine
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/298136a0