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Nucleic Acids Research, 1974, Vol. 1, No. 11 1479-1496
© 1974

Articles

N2-Guanine specific transfer RNA methyltransferase II from rat liver

Jan Kraus* and Matthys Staehelin

Biological Laboratories, Pharmaceutical Department, CIBA-GEIGY Ltd. Basel, Switzerland

Received August 9, 1974.

N2-guanine methyltransferase II was purified from rat liver. This enzyme methylated bulk E. coli tRNA to an extent of 7.6 nmoles of methyl groups/mg tRNA. Oligonucleotide analysis showed that N2-methylated guanosines were present in the modified tRNA in two sequences, namely Y-m2G-Cp and Y-m22G-Cp in the ratio 4:3.

Two pure tRNALeu species, and tRNAfMet from E. coli were methylated with the enzyme to extents of 17, 11, and 8 nmoles of methyl groups incorporated per mg tRNA, respectively. When the methylated tRNAs were analysed no m22G was detected and the m2G occurred in the tRNAs specific for leucine in a Y-m2G-Cp sequence and in the tRNAfMet in a sequence Y-m2G-Up.

It is concluded that the mammalian enzyme specifically recognizes the interstem unpaired guanylate residue between the dihydrouridine arm and the anticodon arm. The absence of any detectable m22G methylation of individual tRNA species is discussed.

*Present address: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, connecticut 06520.


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