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Nucleic Acids Research, 1979, Vol. 6, No. 3 1123-1133
© 1979

Articles

In vitro methylation of yeast tRNAAsp by rat brain cortical tRNA-(adenine-1) methyltransferase

C.E. Salas and G. Dirheimer

Institut de Biologie Moléculaire et Cellulaire du CNRS 15 rue Descartes, 67084 Strasbourg, and Faculté de Pharmacie, Université Louis Pasteur 3 rue de I'Argonne, 67083 Strasbourg, France

Received November 22, 1978. Rat brain cortices from young animals contain large amounts of tRNA(adenine-1)methyltansferase(s). The enzyme(s) can methylate E.coli tRNA and to a lower degree yeast tRNA. Among yeast tRNA species which can be methylated we have selected tRNAAsp as a substrate for the brain enzyme. The digestione of in vitro methylated [Me-3H]-tRNAAsp with pancreatic and/or T1 ribonucleases followed by chromatographies on DEAE-cellulose, 7 M urea, suggested that the methylation of tRNAAsp occurred at a single position within the D-loop. Further digestion of the radioactive oligonucleotide recovered after DEAE-cellulose chromatography by phosphomonoesterase and snake venom phosphodiesterase enzymes followed by bidimensional thin layer chromatography enabled us to determine the Location of the adenine residue which becomes methylated by the brain enzyme. This one resulted to be the adenine 14 in the D-loop of yeast tRNAAsp.


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