Methylation of tRNAAsp by the DNA Methyltransferase Homolog Dnmt2
@article{Goll2006MethylationOT,
title={Methylation of tRNAAsp by the DNA Methyltransferase Homolog Dnmt2},
author={Mary G Goll and Finn Kirpekar and Keith A. Maggert and Jeffrey A. Yoder and Chih-Lin Hsieh and Xiaoyu Zhang and Kent G. Golic and Steven E. Jacobsen and Timothy H Bestor},
journal={Science},
year={2006},
volume={311},
pages={395 - 398}
}The sequence and the structure of DNA methyltransferase-2 (Dnmt2) bear close affinities to authentic DNA cytosine methyltransferases. [] Key Result A combined genetic and biochemical approach revealed that human DNMT2 did not methylate DNA but instead methylated a small RNA; mass spectrometry showed that this RNA is aspartic acid transfer RNA (tRNA(Asp)) and that DNMT2 specifically methylated cytosine 38 in the anticodon loop.
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