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PMID: 7045689 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Nature ·Vol. 298 ·No. 5870 ·1982-07-08 ·Pages 136-40

Starzyk RM, Koontz SW, Schimmel P

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.

MeSH Terms
Alanine-tRNA Ligase/metabolism Amino Acyl-tRNA Synthetases/metabolism Binding Sites Escherichia coli/enzymology Kinetics Protein Binding RNA, Transfer/metabolism Uracil Uridine
Chemicals
Uracil RNA, Transfer Amino Acyl-tRNA Synthetases Alanine-tRNA Ligase Uridine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Starzyk R M
Koontz S W
Schimmel P
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1982-07-08
Pages
136-40
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
NIGMS NIH HHS · GM15539 · United States
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