Methylation of tRNA Asp by the DNA Methyltransferase Homolog Dnmt2
Copyright policy )Methylation of tRNA Asp by the DNA Methyltransferase Homolog Dnmt2
The sequence and the structure of DNA methyltransferase-2 (Dnmt2) bear close affinities to authentic DNA cytosine methyltransferases. 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. The function of DNMT2 is highly conserved, and human DNMT2 protein restored methylation in vitro to tRNA Asp from Dnmt2-deficient strains of mouse, Arabidopsis thaliana, and Drosophila melanogaster in a manner that was dependent on preexisting patterns of modified nucleosides. Indirect sequence recognition is also a feature of eukaryotic DNA methyltransferases, which may have arisen from a Dnmt2-like RNA methyltransferase.
- Columbia University United States
- University of California System United States
- North Carolina State University United States
- University of Utah United States
- University of Southern Denmark Denmark
RNA, Transfer, Asp, Arabidopsis Proteins, Arabidopsis, Transfection, Methylation, Mass Spectrometry, Evolution, Molecular, Cytosine, Mice, Drosophila melanogaster, RNA, Plant, Catalytic Domain, Mutation, Anticodon, NIH 3T3 Cells, Animals, Drosophila Proteins, Humans, DNA (Cytosine-5-)-Methyltransferases
RNA, Transfer, Asp, Arabidopsis Proteins, Arabidopsis, Transfection, Methylation, Mass Spectrometry, Evolution, Molecular, Cytosine, Mice, Drosophila melanogaster, RNA, Plant, Catalytic Domain, Mutation, Anticodon, NIH 3T3 Cells, Animals, Drosophila Proteins, Humans, DNA (Cytosine-5-)-Methyltransferases
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