2.1.1.204: tRNA (cytosine38-C5)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (cytosine38-C5)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.204
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2.1.1.204
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methyltransferases
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n6-methyladenosine
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5-methylcytosine
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mtases
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2'-o-methylation
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epitranscriptomic
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methyltransferase-like
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2'-o-methyltransferase
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piwi-interacting
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mettl16
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spout
- 2.1.1.204
- methyltransferases
- n6-methyladenosine
- 5-methylcytosine
- mtases
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2'-o-methylation
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epitranscriptomic
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methyltransferase-like
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2'-o-methyltransferase
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piwi-interacting
- mettl16
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spout
Reaction
Synonyms
(cytosine-5) RNA methyltransferase, cytosine-5 tRNA methyltransferase, dDnmt2, DNA methyltransferase 2, DnmA, Dnmt2, DNMT2 methyltransferase, EC 2.1.1.29, hDNMT2, Pf-DNMT2, PMT1, pombe methyltransferase 1, RCMT, RNA methyltransferase, spDnmt2, transfer RNA aspartic acid methyltransferase 1, TRDMT1, tRNA aspartic acid methyltransferase 1, tRNA-aspartic acid methyltransferase 1
ECTree
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General Information
General Information on EC 2.1.1.204 - tRNA (cytosine38-C5)-methyltransferase
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evolution
malfunction
metabolism
physiological function
additional information
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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
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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analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp
metabolism
analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp
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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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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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