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. 1986 Feb 11;14(3):1131–1148. doi: 10.1093/nar/14.3.1131

A single tRNA (guanine)-methyltransferase from Tetrahymena with both mono- and di-methylating activity.

M P Reinhart, J M Lewis, P S Leboy
PMCID: PMC339493  PMID: 3081876

Abstract

A tRNA (guanine-2) methyltransferase has been purified to homogeneity from the protozoan Tetrahymena pyriformis. The enzyme methylates purified E. coli tRNAs which have a guanine residue at position 26 from the 5' end; it also methylates tRNA prepared from the m22G- yeast mutant trm 1. This methyltransferase is therefore equivalent to the guanine methyltransferase 2mGII found in mammalian extracts. The purified 2mGII from Tetrahymena is capable of forming both N2-methylguanine and N22-dimethylguanine on a single tRNA isoaccepting species; under conditions of limiting tRNA or long reaction times the predominant product is dimethylguanine. Analysis of the products formed under varying reaction conditions suggests that dimethylguanine formation is a two step process requiring dissociation of the enzyme-monomethylated tRNA intermediate.

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Selected References

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