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S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
S-adenosyl-L-methionine + cytosine38 in tRNA-Asp(GUC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA-Asp(GUC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
S-adenosyl-L-methionine + cytosine38 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp precursor
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp(GTC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp(GTC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
S-adenosyl-L-methionine + cytosine38 in tRNAGlu
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlu
-
25% of the activity with tRNAAsp, the activity with tRNAGlu is not affected by the presence of peptone
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlu
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNGlu
S-adenosyl-L-methionine + cytosine38 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly precursor
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
S-adenosyl-L-methionine + cytosine38 in tRNAVal
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal
assay with tritium-labeled SAM, very low activity
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?
S-adenosyl-L-methionine + cytosine38 in tRNAVal precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal precursor
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?
S-adenosyl-L-methionine + cytosine38 in tRNAVal(AAC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal(AAC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
additional information
?
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S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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-
?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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-
?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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-
?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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-
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-
?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
-
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
-
-
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
RNA methylation by Dnmt2 protects tRNAs against stress-induced cleavage
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-
?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
methylation of cytosine 38 in the anti-codon lopp of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC). Other C38-containing tRNAs-including tRNAMet(ATG), tRNAGlu(CTC), and tRNAHis(GTG) are not detectably methylated in a Dnmt2-dependent manner
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
-
in vitro transcribed tRNAAsp is methylated by DNMT2, albeit at reduced efficiency. Human, mouse, and Dictyostelium tRNA all are substrates for human DNMT2. C79, E119, R160 and R162 are essential for the catalytic mechanism of DNMT2
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
methylates tRNAAsp specifically at cytosine38 in the anticodon loop. Human DNMT2 protein restores methylation in vitro to tRNAAsp from Dnmt2-deficient strains of mouse, Arabidopsis thaliana, and Drosophila melanogaster in a manner that is dependent on preexisting patterns of modified nucleosides. Unmodified tRNAAsp produced by in vitro transcription is not a substrate for DNMT2, which suggests that methylation is guided to cytosine38 by other modifications. Mannosylqueuosine is likely to be involved, because it is unique to tRNAAsp. Analysis of tRNAAsp sequences show complete conservation of the anticodon loop in species whose genomes encode Dnmt2 homologs, but the tRNAAsp anticodon loops in Caenorhabditis elegans and Saccharomyces cerevisiae, which lack Dnmt2 homologs, have diverged
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S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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mapping of the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. tRNA specificity determinants and tRNA binding pocket structure in the DNMT2, overview
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S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
assay with tritium-labeled SAM, specific for tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
Dnmt2-mediated methylation at position C38 in the anticodon loop of tRNA-Asp may have a role in the discrimination between Asp and Glu near-cognate codons
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-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
Dnmt2-mediated methylation at position C38 in the anticodon loop of tRNA-Asp may have a role in the discrimination between Asp and Glu near-cognate codons
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-
?
S-adenosyl-L-methionine + cytosine38 in tRNAGlu
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNGlu
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlu
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNGlu
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
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?
additional information
?
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the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
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?
additional information
?
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Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs
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?
additional information
?
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA
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additional information
?
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DNMT2 induces a conformational change in the tRNA of the DNMT2-tRNA complex
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?
additional information
?
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DNMT2 functions primarily, if not exclusively, as a cytosine 5-methylation RNA methyltransferase with three verified tRNA targets: tRNAAsp, tRNAGly and tRNAVal
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?
additional information
?
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the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
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?
additional information
?
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development and evaluation of 5-azacytidine-mediated RNA immunoprecipitation, a mechanism-based technique in nine steps that exploits the covalent bond formed between an RNA methyltransferase and the cytidine analogue 5-azacytidine to recover RNA targets by immunoprecipitation, overview. High frequency of C>G transversions at the cytosine residues targeted by the enzyme, allowing identification of the specific methylated cytosine(s) in target RNAs. tRNAGly(GCC) bears one DNMT2 target site (C38)
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additional information
?
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DNMT2 is able to methylate the cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl groups to the cytosine residues in the genomic DNA
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additional information
?
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Dnmt2 methylates C38 of tRNA in the bone marrow and modulates the stability and fragmentation of substrate tRNAs
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?
additional information
?
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the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
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?
additional information
?
-
Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA
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additional information
?
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DNMT2 is able to methylate the cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl groups to the cytosine residues in the genomic DNA
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additional information
?
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Dnmt2 methylates C38 of tRNA in the bone marrow and modulates the stability and fragmentation of substrate tRNAs
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?
additional information
?
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the DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA
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additional information
?
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no activity with DNA and other tRNA substrates. Plasmodium falciparum has two isodecoders for valine tRNA, and the very low activity is seen on valine 1 substrate, whereas no activity can be detected on valine 2 tRNA substrate. Purified Pf-TRDMT1 methylates tRNA-Asp at C38 position
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additional information
?
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Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs. Pmt1 shows a striking selectivity for tRNAAsp methylation, which distinguishes Pmt1 from other Dnmt2 homologues. C34 of tRNAPro is a Pmt1- and queuosine-independent tRNA methylation site in Schizosaccharomyces pombe
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additional information
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in vitro methylation activity on tRNAAsp and, to a lesser extent, tRNAGlu. No methylation activity with C38-containing tRNAs for histidine, glutamate, and valine
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additional information
?
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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additional information
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Q34tRNAAsp exhibits an only slightly increased affinity for Dnmt2 in comparison to unmodified G34tRNA
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additional information
?
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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additional information
?
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Q34tRNAAsp exhibits an only slightly increased affinity for Dnmt2 in comparison to unmodified G34tRNA
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additional information
?
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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additional information
?
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Q34tRNAAsp exhibits an only slightly increased affinity for Dnmt2 in comparison to unmodified G34tRNA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
S-adenosyl-L-methionine + cytosine38 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp precursor
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp(GTC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp(GTC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
S-adenosyl-L-methionine + cytosine38 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly precursor
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
S-adenosyl-L-methionine + cytosine38 in tRNAVal precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal precursor
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S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
additional information
?
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S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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S-adenosyl-L-methionine + cytosine38 in G34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in G34tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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?
S-adenosyl-L-methionine + cytosine38 in Q34tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in Q34tRNAAsp
preferred substrate
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
RNA methylation by Dnmt2 protects tRNAs against stress-induced cleavage
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
Dnmt2-mediated methylation at position C38 in the anticodon loop of tRNA-Asp may have a role in the discrimination between Asp and Glu near-cognate codons
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
Dnmt2-mediated methylation at position C38 in the anticodon loop of tRNA-Asp may have a role in the discrimination between Asp and Glu near-cognate codons
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
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?
additional information
?
-
-
the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
-
-
?
additional information
?
-
-
Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs
-
-
?
additional information
?
-
Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA
-
-
-
additional information
?
-
-
DNMT2 functions primarily, if not exclusively, as a cytosine 5-methylation RNA methyltransferase with three verified tRNA targets: tRNAAsp, tRNAGly and tRNAVal
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-
?
additional information
?
-
-
the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
-
-
?
additional information
?
-
Dnmt2 methylates C38 of tRNA in the bone marrow and modulates the stability and fragmentation of substrate tRNAs
-
-
?
additional information
?
-
the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA
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additional information
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Dnmt2 methylates C38 of tRNA in the bone marrow and modulates the stability and fragmentation of substrate tRNAs
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additional information
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the DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA
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additional information
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Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs. Pmt1 shows a striking selectivity for tRNAAsp methylation, which distinguishes Pmt1 from other Dnmt2 homologues. C34 of tRNAPro is a Pmt1- and queuosine-independent tRNA methylation site in Schizosaccharomyces pombe
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additional information
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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additional information
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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additional information
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Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp
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Adenocarcinoma of Lung
RNA methyltransferase METTL3 induces intrinsic resistance to gefitinib by combining with MET to regulate PI3K/AKT pathway in lung adenocarcinoma.
Bone Resorption
Circ_0008542 in osteoblast exosomes promotes osteoclast-induced bone resorption through m6A methylation.
Breast Neoplasms
BCDIN3D RNA methyltransferase stimulates Aldolase C expression and glycolysis through let-7 microRNA in breast cancer cells.
Breast Neoplasms
Elevated expression of RNA methyltransferase BCDIN3D predicts poor prognosis in breast cancer.
Breast Neoplasms
Human BCDIN3D monomethylates cytoplasmic histidine transfer RNA.
Carcinogenesis
METTL14 facilitates global genome repair and suppresses skin tumorigenesis.
Carcinoma
RNA methyltransferase NSUN2 promotes hypopharyngeal squamous cell carcinoma proliferation and migration by enhancing TEAD1 expression in an m5C-dependent manner.
Carcinoma, Ehrlich Tumor
Recognition of the ribosomal RNA structures by purified nucleolar RNA methyltransferase.
Carcinoma, Hepatocellular
RNA methyltransferase NSUN2 promotes growth of hepatocellular carcinoma cells by regulating fizzy-related-1 in vitro and in vivo.
Carcinoma, Hepatocellular
The ATF/CREB site is the key element for transcription of the human RNA methyltransferase like 1(RNMTL1) gene, a newly discovered 17p13.3 gene.
Carcinoma, Hepatocellular
The Role of RNA Methyltransferase METTL3 in Hepatocellular Carcinoma: Results and Perspectives.
Carcinoma, Hepatocellular
[METTL14 as a predictor of postoperative survival outcomes of patients with hepatocellular carcinoma].
Carcinoma, Non-Small-Cell Lung
The RNA Methyltransferase NSUN2 and Its Potential Roles in Cancer.
Cystic Fibrosis
Identification of Aminoglycoside-resistant Pseudomonas aeruginosa producing RmtG 16S ribosomal RNA methyltransferase in a cystic fibrosis patient.
Gastrointestinal Neoplasms
Emerging role of RNA methyltransferase METTL3 in gastrointestinal cancer.
Glioma
Epigenetic loss of RNA-methyltransferase NSUN5 in glioma targets ribosomes to drive a stress adaptive translational program.
Hearing Loss
Auditory Pathology in a Transgenic mtTFB1 Mouse Model of Mitochondrial Deafness.
Infections
Temperature-dependent survival of Turnip crinkle virus-infected arabidopsis plants relies on an RNA silencing-based defense that requires dcl2, AGO2, and HEN1.
Intellectual Disability
Mutation in NSUN2, which encodes an RNA methyltransferase, causes autosomal-recessive intellectual disability.
Lung Neoplasms
The RNA Methyltransferase NSUN2 and Its Potential Roles in Cancer.
Neoplasm Metastasis
NSUN2 modified by SUMO-2/3 promotes gastric cancer progression and regulates mRNA m5C methylation.
Neoplasms
METTL3 expression is associated with glycolysis metabolism and sensitivity to glycolytic stress in hepatocellular carcinoma.
Neoplasms
METTL3?mediated m6A modification of Bcl?2 mRNA promotes non?small cell lung cancer progression.
Neoplasms
NSUN2 modified by SUMO-2/3 promotes gastric cancer progression and regulates mRNA m5C methylation.
Neoplasms
Overexpression of NSUN2 by DNA hypomethylation is associated with metastatic progression in human breast cancer.
Neoplasms
Recognition of the ribosomal RNA structures by purified nucleolar RNA methyltransferase.
Neoplasms
Regulation of telomere homeostasis and genomic stability in cancer by N 6-adenosine methylation (m6A).
Neoplasms
RNA methyltransferase NSUN2 promotes gastric cancer cell proliferation by repressing p57Kip2 by an m5C-dependent manner.
Neoplasms
RNA methyltransferase NSUN2 promotes hypopharyngeal squamous cell carcinoma proliferation and migration by enhancing TEAD1 expression in an m5C-dependent manner.
Neoplasms
The Critical Role of RNA m6A Methylation in Cancer.
Neoplasms
The RNA methyltransferase Misu (NSun2) mediates Myc-induced proliferation and is upregulated in tumors.
Neoplasms
The RNA Methyltransferase NSUN2 and Its Potential Roles in Cancer.
Neoplasms
Ubiquitination-mediated degradation of TRDMT1 regulates homologous recombination and therapeutic response.
Neoplasms
Virion-associated and cellular RNA methylase activity in normal and neoplastic mammary tissue from mammary tumor virus-infected and -uninfected mice.
Osteoarthritis
METTL3 promotes experimental osteoarthritis development by regulating inflammatory response and apoptosis in chondrocyte.
Pancreatic Neoplasms
The RNA methyltransferase NSUN6 suppresses pancreatic cancer development by regulating cell proliferation.
Spinal Dysraphism
An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1).
Squamous Cell Carcinoma of Head and Neck
RNA methyltransferase NSUN2 promotes hypopharyngeal squamous cell carcinoma proliferation and migration by enhancing TEAD1 expression in an m5C-dependent manner.
Stomach Neoplasms
RNA methyltransferase NSUN2 promotes gastric cancer cell proliferation by repressing p57Kip2 by an m5C-dependent manner.
Tuberculosis
A Novel Motif for S-Adenosyl-l-methionine Binding by the Ribosomal RNA Methyltransferase TlyA from Mycobacterium tuberculosis.
Wilms Tumor
mTORC1 promotes cell growth via m6A-dependent mRNA degradation.
Wilms Tumor
mTORC1 stimulates cell growth through SAM synthesis and m6A mRNA-dependent control of protein synthesis.
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evolution
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DNMT2 methylates RNA by employing a DNA methyltransferase-like catalytic mechanism, which is clearly different from the mechanism of other RNA MTases. DNMT2 has changed its substrate specificity from DNA to RNA in the course of its evolution
evolution
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DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain
evolution
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DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain
evolution
DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain
evolution
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identification of single-nucleotide resolution of cytosine 5-methylation sites in non-coding ribosomal RNAs and transfer RNAs of all three subcellular transcriptomes across six diverse species, overview. Both the nucleotide position and percent methylation of tRNAs and rRNAs cytosine 5-methylation sites are conserved across all species analysed, overview
evolution
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the enzyme belongs to the DNMT2 family of cytosine 5-methylation-RNA methyltransferases utilizing only one cysteine in their catalytic pocket
evolution
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the enzyme is a highly conserved cytosine-C5 methyltransferase that introduces the C38 methylation of tRNA-Asp in many species, including lower eukaryotes, plants, insects and humans
evolution
phylogenetic analysis revealed that Plasmodium falciparum TRDMT1 clusters into tRNA specific methyltransferase family. The enzyme structure harbors all the essential motifs for C5 DNA methylation activity as well as tRNA methylation
evolution
the DNMTs encompass three different structural regions: N-terminal regulatory domain, C-terminal catalytic domain and a central linker region. The N-terminal regulatory domain is particularly implicated in determining subcellular localization of the DNMT and in allocating unmethylated DNA strands from hemi-methylated ones. The C-terminal catalytic domain consists of 10 different characteristic motifs, and six of them (I, IV, VI, VIII, IX and X) are evolutionally conserved among mammals. General structure of mammalian DNA methyltransferases (DNMTs), overview. DNMT2 shows structural and functional differences when compared with the other DNMTs, it does not include N-terminal domain, and therefore cannot contribute to de-novo or maintenance methylation process
evolution
the DNMTs encompass three different structural regions: N-terminal regulatory domain, C-terminal catalytic domain and a central linker region. The N-terminal regulatory domain is particularly implicated in determining subcellular localization of the DNMT and in allocating unmethylated DNA strands from hemi-methylated ones. The C-terminal catalytic domain consists of 10 different characteristic motifs, and six of them (I, IV, VI, VIII, IX and X) are evolutionally conserved among mammals. General structure of mammalian DNA methyltransferases (DNMTs), overview. DNMT2 shows structural and functional differences when compared with the other DNMTs, it does not include N-terminal domain, and therefore cannot contribute to de-novo or maintenance methylation process
malfunction
Drosophila Dnmt2 mutants show reduced viability under stress conditions, and Dnmt2 relocalizes to stress granules following heat shock
malfunction
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knockdown of Dnmt2 protein in zebrafish embryos confers differentiation defects in particular organs, including the retina, liver, and brain
malfunction
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methylation at C11 of tRNASer (GCT) shows an inverse correlation to the presence of Pmt1 and queuine in pmt1-mutant cells in that its level increases from 23 to 37% in the absence of Pmt1
malfunction
specific codon mistranslation by tRNAs lacking Dnmt2-dependent methylation causes systematic differences in protein expression, with 153 significantly deregulated proteins among a total of 4094 identified proteins. Enzyme-deficient Dnmt2-/- mice reveal delayed endochondral ossification of the long bones with uantitative differences in the length of the zone of cell maturation and hypertrophy in the epiphyseal plate between wild-type and Dnmt2-/- mice as well as in the length of the trabecular zone between wild-type and Dnmt2-/- mice. The trabecular structures are not only reduced in length but also appear incorrectly interfaced with bone marrow cells. The numbers of capillaries counted in the trabecular zone are significantly reduced. Enzyme-deficient bone marrow cells show an enlarged pool of osteo-progenitors. Haematopoietic phenotype, detailed overview
malfunction
the Dnmt2 knockout mouse model does not exhibit any phenotypic defects in the mouse model. The enzyme knockout causes disruption of RNA methyltransferase activity
malfunction
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the enzyme knockout causes disruption of RNA methyltransferase activity
malfunction
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the enzyme knockout causes disruption of RNA methyltransferase activity
malfunction
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trdmt1/trm4b double mutants are hypersensitive to the antibiotic hygromycin B. Non-methylated C38 in trdmt1-defective plants results in loss of HpyCH4IV restriction site
malfunction
a 30% reduced charging level of tRNA-Asp is observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Synthesis of endogenous proteins with poly-Asp sequences is reduced in Dnmt2 KO cells. Protein degradation does not cause reduction of protein level in Dnmt2 KO cells
malfunction
combined phenotypes for the absence of Dnmt2 and queuosine (Q). Consequences of absence of Dnmt2 in flies: transposon silencing, stress resistance and immune control of pathogens. Drosophila Dnmt2 mutants lack obvious growth or developmental phenotypes. Dnmt2 mutant flies furthermore show increased viral load and have an activated innate immune response. Conversely, Dnmt2 overexpression reduces infection of Drosophila with Wolbachia and reduces rates of cytoplasmic incompatibility caused by Wolbachia. Drosophila lacking Dnmt2 is viable and fertile
malfunction
combined phenotypes for the absence of Dnmt2 and queuosine (Q). Schizosaccharomyces pombe lacking Dnmt2 is viable and fertile
malfunction
combined phenotypes for the absence of Dnmt2 and queuosine (Q). The absence of both Dnmt2 and a second tRNA methyltransferase, NSun2 (EC 2.1.1.202), which generates m5C at other tRNA positions, causes embryonic lethality. The complete absence of m5C in Dnmt2/Nsun2 double mutant cells causes reduced protein synthesis and reduced tRNA levels, which is consistent with a role of m5C in translation as well as in tRNA stability (which is regulated by cleavage). A closer inspection of Dnmt2 mutant mice reveals that they have a delay in endochondral ossification and a reduction in haematopoietic stem and progenitor cell populations. Furthermore, mutant mice have cardiac hypertrophy, though cardiac function seems not to be disturbed. In embryonic stem cells, the absence of Dnmt2 is accompanied by increased activity of RNA polymerase II, which is attributed to decreased levels of non-coding RNAs that exert an inhibitory effect on RNA polymerase II. It is proposed that Dnmt2 methylates and stabilizes these RNAs. Mice lacking Dnmt2 are viable and fertile
malfunction
Dnmt2 knockout mice (Dnmt2-/-) exhibit disruption in the RNA methyltransferase activity
malfunction
mutation in (cytosine-5) RNA methyltransferase Dnmt2, which targets mostly tRNAs, impacts the expression of mobile element-derived sequences and affects DNA repeat integrity in Drosophila melanogaster. Reduced tRNA stability in the RCMT mutant indicates that tRNA-dependent processes affect mobile element expression and DNA repeat stability. Loss of Dnmt2 function causes moderate effects under standard conditions, while heat shock exacerbates these effects. Inefficient silencing of stress-induced transposable elements (TEs) in Dnmt2 mutants, long-lasting TE expression changes in Dnmt2 mutants after heat shock. Dnmt2 mutant phenotype implicated Dnmt2 function in retrotransposon regulation in Drosophila, resulting in silencing defects of long terminal repeat (LTR)-containing transposable elements (TEs) and impaired telomere integrity. P2 expression increases steadily in Dnmt2 mutant males, while expression is only transient in controls (P2). In addition, Dnmt2 mutants displays increasing Inv4 transcript levels (P3). RCMT mutants display genetic changes involving Tag-Inv4. Heat-shock-dependent Inv4 expression is independent of DNA methylation. NSun2 mutants show heat-shock-independent TE expression changes. Dnmt2 mutants accumulate small RNA pathway substrate RNAs, and a catalytically mutant Dnmt2 rescues TE expression changes
malfunction
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combined phenotypes for the absence of Dnmt2 and queuosine (Q). Schizosaccharomyces pombe lacking Dnmt2 is viable and fertile
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malfunction
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combined phenotypes for the absence of Dnmt2 and queuosine (Q). Schizosaccharomyces pombe lacking Dnmt2 is viable and fertile
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malfunction
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specific codon mistranslation by tRNAs lacking Dnmt2-dependent methylation causes systematic differences in protein expression, with 153 significantly deregulated proteins among a total of 4094 identified proteins. Enzyme-deficient Dnmt2-/- mice reveal delayed endochondral ossification of the long bones with uantitative differences in the length of the zone of cell maturation and hypertrophy in the epiphyseal plate between wild-type and Dnmt2-/- mice as well as in the length of the trabecular zone between wild-type and Dnmt2-/- mice. The trabecular structures are not only reduced in length but also appear incorrectly interfaced with bone marrow cells. The numbers of capillaries counted in the trabecular zone are significantly reduced. Enzyme-deficient bone marrow cells show an enlarged pool of osteo-progenitors. Haematopoietic phenotype, detailed overview
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metabolism
analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp
metabolism
analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp
physiological function
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Dnmt2 methylates an RNA species of about 80 bases, consistent with tRNA methylation. Thus, Dnmt2 promotes zebrafish development, likely through cytoplasmic RNA methylation
physiological function
RNA methylation by Dnmt2 protects tRNAs against stress-induced cleavage by ribonuclease
physiological function
Dnmt2 plays an important role in haematopoiesis and define an additional function of C38 tRNA methylation in the discrimination of near-cognate codons, thereby ensuring accurate polypeptide synthesis, role for Dnmt2 in the regulation of codon fidelity. The enzyme prevents tRNA fragmentation. Enzyme Dnmt2 is required for cell differentiation, e.g. of bone marrow mesenchymal stromal cells and for cell-autonomous differentiation during haematopoiesis
physiological function
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Pmt1 provides in vivo tRNA methylation activity that is strongly controlled by nutritional cues
physiological function
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post-transcriptional methylation of RNA cytosine residues to 5-methylcytosine is an important modification that regulates RNA metabolism. Identification of cytosine 5-methylation sites in nuclear, chloroplast and mitochondrial tRNAs. Nuclear tRNA methylation requires two evolutionarily conserved methyltransferases, TRDMT1 and TRM4B, EC 2.1.1.202
physiological function
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The DNMT2 protein methylates C38 of tRNA-Asp and it has a role in cellular physiology and stress response and its expression levels are altered in cancer tissues
physiological function
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though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
physiological function
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though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
physiological function
though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA
physiological function
Dnmt2 proteins are highly conserved (cytosine-5) methyltransferases that methylate specific tRNAs instead of genomic DNA. Dnmt2-mediated effects are mostly heat shock dependent. Connection between Dnmt2 and transposable element (TE) silencing
physiological function
Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp. Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences. Mouse aspartyl-tRNA synthetase shows a 4 to 5fold preference for C38-methylated tRNA-Asp. Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Cytosine-38 methylation of tRNAAsp increases the rate of its aminoacylation
physiological function
Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp. Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences. Proteins containing poly-Asp sequences in the human proteome often have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences. Cytosine-38 methylation of tRNAAsp increases the rate of its aminoacylation
physiological function
enzyme DNMT2 carries out methylation of the cytosine 38 in the anticodon loop of aspartic acid transfer RNA. It is not involved in spermatogenesis
physiological function
enzyme DNMT2 carries out methylation of the cytosine 38 in the anticodon loop of aspartic acid transfer RNA. It is not involved in spermatogenesis
physiological function
enzyme Dnmt2 methylates cytosine at position 38 of tRNAAsp. A correlation between the presence of the hypermodified nucleoside queuosine (Q) at position 34 of tRNAAsp and the Dnmt2 dependent C38 methylation has recently been found in vivo for Schizosaccharomcyces pombe. Dnmt2 shows an increase for in vitro transcribed tRNAAsp containing Q34 compared to the unmodified substrate, structural basis for the Q-dependency, overview. The C38 methylation of tRNAAsp in Schizosaccharomcyces pombe depends on the presence of queuosine (Q), a hypermodified nucleoside at position 34 of tRNAAsp, tRNAAsn, tRNATyr, and tRNAHis10
physiological function
nutritional regulation of Dnmt2 in the fission yeast Schizosaccharomyces pombe, cross-talk between Dnmt2-dependent tRNA methylation and queuosine modification, overview. The presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications, modeling of the functional cooperation between these modifications, overview. The strong Q-dependence observed for Schizosaccharomyces pombe Dnmt2 may be unique to (or strongest in) this organism. Protection of tRNAs from endonucleolytic cleavage by Q and m5C38 modification
physiological function
the presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications, modeling of the functional cooperation between these modifications, overview. Dnmt2 is required for silencing of Invader4 retrotransposons, but not for pericentric heterochromatin silencing. Heat shock of flies is accompanied by the appearance of tRNA fragments whose levels are increased in the absence of Dnmt2, showing a protective role for Dnmt2-mediated methylation against endonucleolytic cleavage. One function of Dnmt2 enzymes may be to suppress aberrant tRNA fragmentation and thus to ensure the correct regulation of siRNA pathways under stressful conditions. Protection of tRNAs from endonucleolytic cleavage by Q and m5C38 modification
physiological function
the presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications, modeling of the functional cooperation between these modifications, overview. Protection of tRNAs from endonucleolytic cleavage by Q and m5C38 modification
physiological function
TRDMT1, a conserved homolog of DNA methyltransferase DNMT2, specifically methylates endogenous aspartic acid tRNA, but not DNA. TRDMT1 mediated C38 methylation of aspartic acid tRNA might play a critical role by translational regulation of important proteins and modulate the pathogenicity of the malarial parasite. Methylation of aspartic acid tRNA can modulate Plasmodium falciparum pathogenicity through translational regulation of functionally important proteins. 5-Methyl cytosines are present only on the RNA and not on the DNA of Plasmodium falciparum
physiological function
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nutritional regulation of Dnmt2 in the fission yeast Schizosaccharomyces pombe, cross-talk between Dnmt2-dependent tRNA methylation and queuosine modification, overview. The presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications, modeling of the functional cooperation between these modifications, overview. The strong Q-dependence observed for Schizosaccharomyces pombe Dnmt2 may be unique to (or strongest in) this organism. Protection of tRNAs from endonucleolytic cleavage by Q and m5C38 modification
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physiological function
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enzyme Dnmt2 methylates cytosine at position 38 of tRNAAsp. A correlation between the presence of the hypermodified nucleoside queuosine (Q) at position 34 of tRNAAsp and the Dnmt2 dependent C38 methylation has recently been found in vivo for Schizosaccharomcyces pombe. Dnmt2 shows an increase for in vitro transcribed tRNAAsp containing Q34 compared to the unmodified substrate, structural basis for the Q-dependency, overview. The C38 methylation of tRNAAsp in Schizosaccharomcyces pombe depends on the presence of queuosine (Q), a hypermodified nucleoside at position 34 of tRNAAsp, tRNAAsn, tRNATyr, and tRNAHis10
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physiological function
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nutritional regulation of Dnmt2 in the fission yeast Schizosaccharomyces pombe, cross-talk between Dnmt2-dependent tRNA methylation and queuosine modification, overview. The presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications, modeling of the functional cooperation between these modifications, overview. The strong Q-dependence observed for Schizosaccharomyces pombe Dnmt2 may be unique to (or strongest in) this organism. Protection of tRNAs from endonucleolytic cleavage by Q and m5C38 modification
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physiological function
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enzyme Dnmt2 methylates cytosine at position 38 of tRNAAsp. A correlation between the presence of the hypermodified nucleoside queuosine (Q) at position 34 of tRNAAsp and the Dnmt2 dependent C38 methylation has recently been found in vivo for Schizosaccharomcyces pombe. Dnmt2 shows an increase for in vitro transcribed tRNAAsp containing Q34 compared to the unmodified substrate, structural basis for the Q-dependency, overview. The C38 methylation of tRNAAsp in Schizosaccharomcyces pombe depends on the presence of queuosine (Q), a hypermodified nucleoside at position 34 of tRNAAsp, tRNAAsn, tRNATyr, and tRNAHis10
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physiological function
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Dnmt2 plays an important role in haematopoiesis and define an additional function of C38 tRNA methylation in the discrimination of near-cognate codons, thereby ensuring accurate polypeptide synthesis, role for Dnmt2 in the regulation of codon fidelity. The enzyme prevents tRNA fragmentation. Enzyme Dnmt2 is required for cell differentiation, e.g. of bone marrow mesenchymal stromal cells and for cell-autonomous differentiation during haematopoiesis
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additional information
enzyme Dnmt2 from Schizosaccharomyces pombe contains the entire active site loop. The interaction with tRNA is analyzed by means of mass spectrometry using UV cross-linked Dnmt2-tRNA complex. Cross-link data and computational docking of Dnmt2 and tRNAAsp reveal Q34 positioned adjacent to the S-adenosylmethionine occupies the active site, suggesting that the observed increase of Dnmt2 catalytic efficiency by queuine originates from optimal positioning of the substrate molecules and residues relevant for methyl transfer. Observation of displacement of the cytosine from the codon-anticodon helix and distortion of the latter, hinting to a role of the Q-modification in translational accuracy. Analysis of spDnmt2 electrostatic surface potentials unveils predominantly positively charged surface around the SAH indicating possible interaction with the tRNA phosphate backbone. But structure exposes a strongly negatively charged cavity in close proximity to the sulfur of S-adenosyl-L-homocysteine formed by the conserved catalytic residue Glu121
additional information
variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation
additional information
variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation
additional information
variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation
additional information
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variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation
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additional information
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enzyme Dnmt2 from Schizosaccharomyces pombe contains the entire active site loop. The interaction with tRNA is analyzed by means of mass spectrometry using UV cross-linked Dnmt2-tRNA complex. Cross-link data and computational docking of Dnmt2 and tRNAAsp reveal Q34 positioned adjacent to the S-adenosylmethionine occupies the active site, suggesting that the observed increase of Dnmt2 catalytic efficiency by queuine originates from optimal positioning of the substrate molecules and residues relevant for methyl transfer. Observation of displacement of the cytosine from the codon-anticodon helix and distortion of the latter, hinting to a role of the Q-modification in translational accuracy. Analysis of spDnmt2 electrostatic surface potentials unveils predominantly positively charged surface around the SAH indicating possible interaction with the tRNA phosphate backbone. But structure exposes a strongly negatively charged cavity in close proximity to the sulfur of S-adenosyl-L-homocysteine formed by the conserved catalytic residue Glu121
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additional information
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variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation
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additional information
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enzyme Dnmt2 from Schizosaccharomyces pombe contains the entire active site loop. The interaction with tRNA is analyzed by means of mass spectrometry using UV cross-linked Dnmt2-tRNA complex. Cross-link data and computational docking of Dnmt2 and tRNAAsp reveal Q34 positioned adjacent to the S-adenosylmethionine occupies the active site, suggesting that the observed increase of Dnmt2 catalytic efficiency by queuine originates from optimal positioning of the substrate molecules and residues relevant for methyl transfer. Observation of displacement of the cytosine from the codon-anticodon helix and distortion of the latter, hinting to a role of the Q-modification in translational accuracy. Analysis of spDnmt2 electrostatic surface potentials unveils predominantly positively charged surface around the SAH indicating possible interaction with the tRNA phosphate backbone. But structure exposes a strongly negatively charged cavity in close proximity to the sulfur of S-adenosyl-L-homocysteine formed by the conserved catalytic residue Glu121
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C292A
-
about 3fold reduction in RNA binding affinity. Significant residual activity
D217H
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D226Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D255Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E185K
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E202Q
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E317G
-
site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme
E63K
-
site-directed mutagenesis, the mutation causes a twofold increase in activity compared to the wild-type enzyme
G155S
-
site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
G155V
-
site-directed mutagenesis, almost inactive mutant
K122A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K168A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K196A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K241A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K251A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K254A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K271A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K295A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K346A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K363A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K367A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K387A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
L257V
-
site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
M72I
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
N264S
-
site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme
R240A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
R275A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R288A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R289A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R369A
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R371A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R371H
-
site-directed mutagenesis, almost inactive mutant
R84A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R95A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
C79A
-
site-directed mutagenesis, inactive mutant
C79A
-
about 3fold reduction in RNA binding affinity. No detectable in vitro methylation activity
E119A
-
site-directed mutagenesis, inactive mutant
E119A
-
mutant binds stronger to RNA than wild-type. No detectable in vitro methylation activity
R160A
-
site-directed mutagenesis, inactive mutant
R160A
-
no detectable in vitro methylation activity
R162A
-
site-directed mutagenesis, inactive mutant
R162A
-
no detectable in vitro methylation activity
additional information
-
generation of a DnmA-deletion mutant
additional information
homozygous Dnmt2-null mutations are viable and fertile, long-term cultivation of Dnmt2 mutant animals might introduce genomic changes accounting for some of the observed phenotypes. Generation of Dnmt2 mutant allele (Dnmt2DELTA5.4), which shows loss of RNA methylation at known tRNA substrates. Catalytically mutant Dnmt2 rescues transposable element (TE) expression changes. Recombinant ectopic expression of the catalytically inactive mutant Dnmt2, which does not reconstitute tRNA methylation, also normalizes TE expression levels. RNAi-mediated knockdown of Dnmt2 in follicle cells. Spliced Gypsy mRNA is significantly elevated in Dnmt2 mutants after heat shock, but not in controls, functional Gypsy retroviral particles can be formed in Dnmt2 mutants. Specific eccDNAs accumulate in RCMT mutants. RCMT mutants display reduced tRNA stability and tRNA abundance
additional information
generation of Dnmt2 knockout (KO) cells
additional information
-
generation of Dnmt2 knockout (KO) cells
additional information
generation of Dnmt2/- knockout mice
additional information
generation of Dnmt2 knockout mice
additional information
generation of Dnmt2 knockout murine embryonic fibroblast cells
additional information
-
generation of Dnmt2 knockout murine embryonic fibroblast cells
additional information
-
generation of Dnmt2/- knockout mice
-
additional information
construction of enzyme mutant Pf-NDELTATRDMT1 lacking the N-terminus. The Pf-NDELTATRDMT1 protein consists of motifs specific for both DNA and tRNA methyltransferases, substrate specificity analysis reveals that no DNA methylation activity can be detected, but Pf-NDELTATRDMT1 methylates only tRNA-Asp and very weakly tRNA-Val
additional information
-
generation of a Prmt1-deletion mutant
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Rai, K.; Chidester, S.; Zavala, C.V.; Manos, E.J.; James, S.R.; Karpf, A.R.; Jones, D.A.; Cairns, B.R.
Dnmt2 functions in the cytoplasm to promote liver, brain, and retina development in zebrafish
Genes Dev.
21
261-266
2007
Danio rerio
brenda
Schaefer, M.; Pollex, T.; Hanna, K.; Tuorto, F.; Meusburger, M.; Helmm M.; Lyko, F.
RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage
Genes Dev.
24
1590-1595
2010
Drosophila melanogaster (Q9U6H7)
brenda
Schaefer, M.; Steringer, J.P.; Lyko, F.
The Drosophila cytosine-5 methyltransferase Dnmt2 is associated with the nuclear matrix and can access DNA during mitosis
PLoS One
3
e1414
2008
Drosophila melanogaster
brenda
Jurkowski, T.P.; Meusburger, M.; Phalke, S.; Helm, M.; Nellen, W.; Reuter, G.; Jeltsch, A.
Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism
RNA
14
1663-1670
2008
Drosophila melanogaster, Homo sapiens
brenda
Goll, M.G.; Kirpekar, F.; Maggert, K.A.; Yoder, J.A.; Hsieh, C.L.; Zhang, X.; Golic, K.G.; Jacobsen, S.E.; Bestor, T.H.
Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2
Science
311
395-398
2006
Homo sapiens (O14717), Homo sapiens
brenda
Jurkowski, T.P.; Shanmugam, R.; Helm, M.; Jeltsch, A.
Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase
Biochemistry
51
4438-4444
2012
Homo sapiens
brenda
Elhardt, W.; Shanmugam, R.; Jurkowski, T.P.; Jeltsch, A.
Somatic cancer mutations in the DNMT2 tRNA methyltransferase alter its catalytic properties
Biochimie
112
66-72
2015
Homo sapiens
brenda
Uysal, F.; Akkoyunlu, G.; Ozturk, S.
Dynamic expression of DNA methyltransferases (DNMTs) in oocytes and early embryos
Biochimie
116
103-113
2015
Bos taurus, Homo sapiens, Mus musculus (O55055)
brenda
Burgess, A.; David, R.; Searle, I.
Conservation of tRNA and rRNA 5-methylcytosine in the kingdom Plantae
BMC Plant Biol.
15
199
2015
Arabidopsis thaliana
brenda
Tuorto, F.; Herbst, F.; Alerasool, N.; Bender, S.; Popp, O.; Federico, G.; Reitter, S.; Liebers, R.; Stoecklin, G.; Groene, H.J.; Dittmar, G.; Glimm, H.; Lyko, F.
The tRNA methyltransferase Dnmt2 is required for accurate polypeptide synthesis during haematopoiesis
EMBO J.
34
2350-2362
2015
Mus musculus (O55055), Mus musculus C57BL/6 (O55055)
brenda
Militello, K.T.; Chen, L.M.; Ackerman, S.E.; Mandarano, A.H.; Valentine, E.L.
A map of 5-methylcytosine residues in Trypanosoma brucei tRNA revealed by sodium bisulfite sequencing
Mol. Biochem. Parasitol.
193
122-126
2014
no activity in Trypanosoma brucei
brenda
Khoddami, V.; Cairns, B.R.
Identification of direct targets and modified bases of RNA cytosine methyltransferases
Nat. Biotechnol.
31
458-464
2013
Homo sapiens
brenda
Mueller, M.; Hartmann, M.; Schuster, I.; Bender, S.; Thuering, K.L.; Helm, M.; Katze, J.R.; Nellen, W.; Lyko, F.; Ehrenhofer-Murray, A.E.
Dynamic modulation of Dnmt2-dependent tRNA methylation by the micronutrient queuine
Nucleic Acids Res.
43
10952-10962
2015
Dictyostelium discoideum, Schizosaccharomyces pombe
brenda
Govindaraju, G.; Jabeena, C.A.; Sethumadhavan, D.V.; Rajaram, N.; Rajavelu, A.
DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA
Biochim. Biophys. Acta
1860
1047-1057
2017
Plasmodium falciparum (Q8IBI4)
brenda
Ehrenhofer-Murray, A.E.
Cross-talk between Dnmt2-dependent tRNA methylation and queuosine modification
Biomolecules
7
14
2017
no activity in Saccharomyces cerevisiae, Mus musculus (O55055), Schizosaccharomyces pombe (P40999), Drosophila melanogaster (Q9VKB3), Schizosaccharomyces pombe ATCC 24843 (P40999), Schizosaccharomyces pombe 972 (P40999)
brenda
Shanmugam, R.; Fierer, J.; Kaiser, S.; Helm, M.; Jurkowski, T.P.; Jeltsch, A.
Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences
Cell Discov.
1
15010
2015
Homo sapiens (O14717), Homo sapiens, Mus musculus (O55055), Mus musculus
brenda
Genenncher, B.; Durdevic, Z.; Hanna, K.; Zinkl, D.; Mobin, M.B.; Senturk, N.; Da Silva, B.; Legrand, C.; Carre, C.; Lyko, F.; Schaefer, M.
Mutations in cytosine-5 tRNA methyltransferases impact mobile element expression and genome stability at specific DNA repeats
Cell Rep.
22
1861-1874
2018
Drosophila melanogaster (Q9U6H7)
brenda
Mueller, M.; Hartmann, M.; Schuster, I.; Bender, S.; Thuering, K.L.; Helm, M.; Katze, J.R.; Nellen, W.; Lyko, F.; Ehrenhofer-Murray, A.E.
Dynamic modulation of Dnmt2-dependent tRNA methylation by the micronutrient queuine
Nucleic Acids Res.
43
10952-10962
2015
Schizosaccharomyces pombe (P40999)
brenda
Uysal, F.; Akkoyunlu, G.; Ozturk, S.
DNA methyltransferases exhibit dynamic expression during spermatogenesis
Reprod. Biomed. Online
33
690-702
2016
Homo sapiens (O14717), Mus musculus (O55055)
brenda
Johannsson, S.; Neumann, P.; Wulf, A.; Welp, L.M.; Gerber, H.D.; Krull, M.; Diederichsen, U.; Urlaub, H.; Ficner, R.
Structural insights into the stimulation of S. pombe Dnmt2 catalytic efficiency by the tRNA nucleoside queuosine
Sci. Rep.
8
8880
2018
Schizosaccharomyces pombe (P40999), Schizosaccharomyces pombe ATCC 24843 (P40999), Schizosaccharomyces pombe 972 (P40999)
brenda