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Nucleic Acids Research, 1978, Vol. 5, No. 3 1041-1058
© 1978

Articles

The identification of the tRNA substrates for the supK tRNA methylase

William T. Pope, Anne Brown and Robert H. Reeves

Department of Chemistry, and Institute of Molecular Biophysics, Florida State University Tallahassee, FL 32306, USA

Received January 14, 1978. Purified preparations of the tRNA methylase deficient in supK strains of Salmonella typhimurium transfer methyl groups from S-adenosylmethionine (SAM) to at least two tRNA species, an alanine tRNA and a serine tRNA. The identity of the tRNA substrates for this enzyme was determined by a change in the elution position of the methyl-labeled tRNA from BND-cellulose columns before and after aminoacylation with a specific amino acid followed by derivatization of the free primary amino group with phenoxy- or naphthoxyacetate. The radioactive methyl group enzymatically added to these tRNAs is both acid and base labile and can be hydrolyzed to a volatile product at pHs above 7.5 and also at pH 1. The methylated 3'-nucleo-tide isolated from digested tRNA is a pyrimidine derivative and chromatographs like a modified uridylic acid. Its identity has not been established, but it is likely that it corresponds to the methyl ester of V, uridin-5-oxyacetic acid.


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S. J. NASVALL, P. CHEN, and G. R. BJORK
The modified wobble nucleoside uridine-5-oxyacetic acid in tRNAProcmo5UGG promotes reading of all four proline codons in vivo
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