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Literature summary for 2.1.1.204 extracted from
- Cross-talk between Dnmt2-dependent tRNA methylation and queuosine modification (2017), Biomolecules, 7, 14 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Queuine, the respective base, is a hypermodified guanine analogue that is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it themselves, but rather salvage it from food or from gut microbes. The queuine obtained from these sources comes from the breakdown of tRNAs, where the queuine ultimately is synthesized by bacteria. Queuine thus has been termed a micronutrient | Mus musculus | |
| additional information | the presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Queuine, the respective base, is a hypermodified guanine analogue that is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it themselves, but rather salvage it from food or from gut microbes. The queuine obtained from these sources comes from the breakdown of tRNAs, where the queuine ultimately is synthesized by bacteria. Queuine thus has been termed a micronutrient | Schizosaccharomyces pombe | |
| additional information | the presence of the nucleotide queuosine (Q) in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro. Queuine, the respective base, is a hypermodified guanine analogue that is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it themselves, but rather salvage it from food or from gut microbes. The queuine obtained from these sources comes from the breakdown of tRNAs, where the queuine ultimately is synthesized by bacteria. Queuine thus has been termed a micronutrient | Drosophila melanogaster |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Schizosaccharomyces pombe | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | ? | - |
- |
 |
| additional information | Mus musculus | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA | ? | - |
- |
|
| additional information | Drosophila melanogaster | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA | ? | - |
- |
|
| additional information | Schizosaccharomyces pombe ATCC 24843 | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | ? | - |
- |
|
| additional information | Schizosaccharomyces pombe 972 | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | ? | - |
- |
|
| S-adenosyl-L-methionine + cytosine38 in tRNA | Mus musculus | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | Schizosaccharomyces pombe | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | Drosophila melanogaster | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | Schizosaccharomyces pombe ATCC 24843 | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | Schizosaccharomyces pombe 972 | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Mus musculus | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Schizosaccharomyces pombe | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Drosophila melanogaster | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Schizosaccharomyces pombe ATCC 24843 | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Schizosaccharomyces pombe 972 | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | Q9VKB3 | - |
- |
| Mus musculus | O55055 | - |
- |
| no activity in Saccharomyces cerevisiae | - |
- |
- |
| Schizosaccharomyces pombe | P40999 | - |
- |
| Schizosaccharomyces pombe 972 | P40999 | - |
- |
| Schizosaccharomyces pombe ATCC 24843 | P40999 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | Schizosaccharomyces pombe | ? | - |
- |
|
| additional information | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA | Mus musculus | ? | - |
- |
|
| additional information | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. Dnmt2 binds to viral RNA | Drosophila melanogaster | ? | - |
- |
|
| additional information | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | Schizosaccharomyces pombe ATCC 24843 | ? | - |
- |
|
| additional information | Dnmt2 enzymes are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp | Schizosaccharomyces pombe 972 | ? | - |
- |
|
| S-adenosyl-L-methionine + cytosine38 in tRNA | - |
Mus musculus | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | - |
Schizosaccharomyces pombe | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | - |
Drosophila melanogaster | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | - |
Schizosaccharomyces pombe ATCC 24843 | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNA | - |
Schizosaccharomyces pombe 972 | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Mus musculus | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Schizosaccharomyces pombe | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Drosophila melanogaster | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Schizosaccharomyces pombe ATCC 24843 | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Schizosaccharomyces pombe 972 | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Dnmt2 | - |
no activity in Saccharomyces cerevisiae |
| Dnmt2 | - |
Mus musculus |
| Dnmt2 | - |
Schizosaccharomyces pombe |
| Dnmt2 | - |
Drosophila melanogaster |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Mus musculus | |
| S-adenosyl-L-methionine | - |
Schizosaccharomyces pombe | |
| S-adenosyl-L-methionine | - |
Drosophila melanogaster | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Drosophila melanogaster |
| malfunction | combined phenotypes for the absence of Dnmt2 and queuosine (Q). Schizosaccharomyces pombe lacking Dnmt2 is viable and fertile | Schizosaccharomyces pombe |
| 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 | Mus musculus |
| additional information | variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation | Mus musculus |
| additional information | variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation | Schizosaccharomyces pombe |
| additional information | variations in queuosine (Q) levels during development and in different organs. Organismal roles for tRNA queuosinylation | Drosophila melanogaster |
| 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 | Schizosaccharomyces pombe |
| 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 | Drosophila melanogaster |
| 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 | Mus musculus |
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