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. 1974 Nov;1(11):1479–1496. doi: 10.1093/nar/1.11.1479

N2-Guanine specific transfer RNA methyltransferase II from rat liver

Jan Kraus 1, Matthys Staehelin 1
PMCID: PMC343425  PMID: 10793704

Abstract

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 tRNAMetf 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 tRNAMetf 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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