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S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
S-adenosyl-L-methionine + guanine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAAsp
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?
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
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?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
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?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
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?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
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-
?
S-adenosyl-L-methionine + guanine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNATrp
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?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
additional information
?
-
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the enzyme is specific for guanine9 in tRNA, does not catalyse methylation of adenine9 in tRNA
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
formation of N1-methylguanine9 in tRNA(Asp) from Thermococcus kodakaraensis that contains a guanosine at position 9. The enzyme forms approximately the same amount of m1A and m1G when the tRNA of the yeast strain Y16243 is used as substrate. Given that occurrence of A9 and G9 in this tRNA population is almost equal (about 50% each) this result indicates that the enzyme TK0422p does not show any preference for one of these two nucleosides. The ratio m1A/m1G formed from Escherichia coli tRNA is higher than that with tRNA from the yeast Y16243 strain. This is consistent with the fact that there are about two times more tRNAs with A9 than with G9 in Escherichia coli. The enzyme is active in a pH range 5.5-9.75. The intensity of m1A and m1G spots varies greatly as a function of the pH. At pH 5.5, m1A MTase activity of TK0422p is predominant over m1G. At pH 7 or higher, both m1A and m1G are detected, m1G intensity growing with increasing pH
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S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
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-
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?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
tRNA substrate from Thermococcus kodakarensis
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?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
-
tRNA substrate from Thermococcus kodakarensis
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA substrate from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
-
tRNA substrate from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
tRNA substrate from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
-
tRNA substrate from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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?
additional information
?
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substrate specificity analysis in vivo, overview
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additional information
?
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substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10A displays robust activity on every tested G9-containing tRNA from either humans or Saccharomyces cerevisiae, similar to Saccharomyces cerevisiae ScTrm10. hTRMT10B, and not hTRMT10A, is indeed capable of catalyzing m1A9 methylation on tRNAAsp in vitro, while hTRMT10B has the sole responsibility for generating the m1A9 modification. hTRMT10A displays higher in vitro catalytic rates than hTRMT10B
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additional information
?
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substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10A displays robust activity on every tested G9-containing tRNA from either humans or Saccharomyces cerevisiae, similar to Saccharomyces cerevisiae ScTrm10. hTRMT10B, and not hTRMT10A, is indeed capable of catalyzing m1A9 methylation on tRNAAsp in vitro, while hTRMT10B has the sole responsibility for generating the m1A9 modification. hTRMT10A displays higher in vitro catalytic rates than hTRMT10B
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additional information
?
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the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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additional information
?
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the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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additional information
?
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the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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?
additional information
?
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there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
-
the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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additional information
?
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usage of [alpha-32P]-labeled tRNA substrates. The enzyme shows activity with both guanine9 and adenine9 containing tRNAs for methylation on N1. Bifunctional enzymes (catalyzing both m1A9 and m1G9) share the same rate-determining step for methylation as the monofunctional enzyme, these enzymes would also exhibit a different pattern of pH dependence for the two methylation reactions because of the difference in N1 pKa between adenine versus guanine
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additional information
?
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usage of [alpha-32P]-labeled tRNA substrates. The enzyme shows activity with both guanine9 and adenine9 containing tRNAs for methylation on N1. Bifunctional enzymes (catalyzing both m1A9 and m1G9) share the same rate-determining step for methylation as the monofunctional enzyme, these enzymes would also exhibit a different pattern of pH dependence for the two methylation reactions because of the difference in N1 pKa between adenine versus guanine
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additional information
?
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the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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-
additional information
?
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usage of [alpha-32P]-labeled tRNA substrates. The enzyme shows activity with both guanine9 and adenine9 containing tRNAs for methylation on N1. Bifunctional enzymes (catalyzing both m1A9 and m1G9) share the same rate-determining step for methylation as the monofunctional enzyme, these enzymes would also exhibit a different pattern of pH dependence for the two methylation reactions because of the difference in N1 pKa between adenine versus guanine
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additional information
?
-
the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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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 + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
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?
S-adenosyl-L-methionine + guanine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAAsp
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?
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
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?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
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?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
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?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
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?
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
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?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
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?
S-adenosyl-L-methionine + guanine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNATrp
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?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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?
additional information
?
-
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
additional information
?
-
substrate specificity analysis in vivo, overview
-
-
?
additional information
?
-
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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-
?
additional information
?
-
-
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acidosis, Lactic
Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies.
Carcinogenesis
m1A Regulator TRMT10C Predicts Poorer Survival and Contributes to Malignant Behavior in Gynecological Cancers.
Deafness
Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies.
Diabetes Mellitus
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Diabetes Mellitus
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Diabetes Mellitus
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Epilepsy
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Hypoglycemia
Expanding the Phenotype of TRMT10A Mutations: Case Report and a Review of the Existing Cases.
Insulin Resistance
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Intellectual Disability
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Intellectual Disability
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Microcephaly
Case Report: Compound heterozygous nonsense mutations in TRMT10A are associated with microcephaly, delayed development, and periventricular white matter hyperintensities.
Microcephaly
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Microcephaly
Pancreatic ?-cell tRNA hypomethylation and fragmentation link TRMT10A deficiency with diabetes.
Microcephaly
TRMT10A dysfunction is associated with abnormalities in glucose homeostasis, short stature and microcephaly.
Microcephaly
TRMT10A mutation in a child with diabetes, short stature, microcephaly and hypoplastic kidneys.
Microcephaly
tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans.
Microcephaly
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Mitochondrial Diseases
Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies.
Muscle Hypotonia
Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies.
Neoplasms
m1A Regulator TRMT10C Predicts Poorer Survival and Contributes to Malignant Behavior in Gynecological Cancers.
Ovarian Neoplasms
m1A Regulator TRMT10C Predicts Poorer Survival and Contributes to Malignant Behavior in Gynecological Cancers.
Puberty, Delayed
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
trna (guanine9-n1)-methyltransferase deficiency
Pancreatic ?-cell tRNA hypomethylation and fragmentation link TRMT10A deficiency with diabetes.
trna (guanine9-n1)-methyltransferase deficiency
TRMT10A dysfunction is associated with abnormalities in glucose homeostasis, short stature and microcephaly.
trna (guanine9-n1)-methyltransferase deficiency
tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans.
Uterine Cervical Neoplasms
m1A Regulator TRMT10C Predicts Poorer Survival and Contributes to Malignant Behavior in Gynecological Cancers.
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physiological function
robust activity for hTRMT10A as a tRNAAsp-specific m1A9 methyltransferase, it is the relevant enzyme responsible for the m1A9 modification in humans. Inability of hTRMT10A to catalyze any detectable m1A9 modification
evolution
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea
evolution
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea. The tRNA methyltransferase Trm10 is a highly conserved protein both necessary and sufficient to catalyze all known instances of m1G9 modification in yeast
evolution
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
evolution
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
evolution
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
evolution
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
evolution
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
evolution
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
evolution
the enzyme belongs to the tRNA m1R9 methyltransferase (Trm10) family, which is conserved throughout eukarya and archaea. Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B. hTRMT10A and hTRMT10B are not biochemically redundant. hTRMT10A is the de facto methyltransferase responsible for all m1G9 formation on cytosolic tRNA, and hTRMT10B has a much more limited and specific role in tRNA processing in humans
evolution
tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout eukarya and archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a distinct mechanism of catalysis. Sequence comparison of human TRMT10A and yeast Trm10. Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD
evolution
tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout eukarya and archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a distinct mechanism of catalysis. Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD
evolution
-
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
-
evolution
-
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
-
evolution
-
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
-
evolution
-
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
-
evolution
-
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
-
evolution
-
tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout eukarya and archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a distinct mechanism of catalysis. Sequence comparison of human TRMT10A and yeast Trm10. Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD
-
evolution
-
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein
-
malfunction
guanine9 methylation activity is not detectable in trm10-DELTA/trm10-DELTA strain
malfunction
TRMT10A silencing induces human beta-cell apoptosis.. TRMT10A deficiency negatively affects beta-cell mass and the pool of neurons in the developing brain. A nonsense mutation R127stop in the enzyme is involved in the syndrome of young onset diabetes, short stature and microcephaly (small brain size) with intellectual disability in a large consanguineous family, TRMT10A mRNA and protein are absent in cells from affected siblings, phenotype, overview. Patients are homozygous for a nonsense mutation in TRMT10A and lose TRMT10A expression
malfunction
several disease states correlate with deficiency in the human homologue TRMT10A, mostly characterized by neurological and glucose metabolic defects, despite the presence of another cytoplasmic enzyme, TRMT10B
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
-
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
-
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
-
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
-
metabolism
-
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms
-
additional information
enzyme overall structure analysis, active site structure, overview
additional information
-
enzyme overall structure analysis, active site structure, overview
additional information
enzyme overall structure analysis, active site structure, overview
additional information
-
enzyme overall structure analysis, active site structure, overview
additional information
residue G202 is important for catalytic activity regardless of the target purine of the tRNA species to be modified
additional information
-
residue G202 is important for catalytic activity regardless of the target purine of the tRNA species to be modified
additional information
the proposed aspartate general base D210 is not critical for methylation activity, mechanism of m1G9 methylation by Trm10. The pH-rate analysis suggests that D210 and other conserved carboxylate-containing residues at the active site collaborate to establish an active site environment that promotes a single ionization that is required for catalysis. Active site residues structure-function analysis
additional information
-
the proposed aspartate general base D210 is not critical for methylation activity, mechanism of m1G9 methylation by Trm10. The pH-rate analysis suggests that D210 and other conserved carboxylate-containing residues at the active site collaborate to establish an active site environment that promotes a single ionization that is required for catalysis. Active site residues structure-function analysis
additional information
the proposed aspartate general base D210 is not critical for methylation activity, mechanism of m1G9 methylation by Trmt10A. The pH-rate analysis suggests that D210 and other conserved carboxylate-containing residues at the active site collaborate to establish an active site environment that promotes a single ionization that is required for catalysis. Active site residues structure-function analysis
additional information
tRNA recognition by Trm10 enzymes, overview
additional information
tRNA recognition by Trm10 enzymes, overview
additional information
tRNA recognition by Trm10 enzymes, overview
additional information
tRNA recognition by Trm10 enzymes, overview
additional information
tRNA recognition by Trm10 enzymes, overview
additional information
-
tRNA recognition by Trm10 enzymes, overview
-
additional information
-
tRNA recognition by Trm10 enzymes, overview
-
additional information
-
enzyme overall structure analysis, active site structure, overview
-
additional information
-
tRNA recognition by Trm10 enzymes, overview
-
additional information
-
tRNA recognition by Trm10 enzymes, overview
-
additional information
-
the proposed aspartate general base D210 is not critical for methylation activity, mechanism of m1G9 methylation by Trm10. The pH-rate analysis suggests that D210 and other conserved carboxylate-containing residues at the active site collaborate to establish an active site environment that promotes a single ionization that is required for catalysis. Active site residues structure-function analysis
-
additional information
-
tRNA recognition by Trm10 enzymes, overview
-
additional information
-
residue G202 is important for catalytic activity regardless of the target purine of the tRNA species to be modified
-
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D210N
site-directed mutagenesis, the mutant is resistant to 5-fluorouracil similarly to the wild-type enzyme
G206R
site-directed mutagenesis, inactive variant of hTRMT10A with abolished methylation activity, likely due to an inability to bind cofactor SAM
R127stop
naturally occuring nonsene mutation involved in the syndrome of young onset diabetes
D210A
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
D210K
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
N212A
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
D210A
-
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
-
D210K
-
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
-
D210N
-
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
-
D207N
site-directed mutagenesis, inactive mutant
K110E/R121E/R127E
site-directed mutagenesis, inactive mutant
K153E/R147E
site-directed mutagenesis, inactive mutant
K208A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 28% reduced activity compared to the wild-type enzyme
N209A
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
Q118A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, inactive mutant
T244A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 65% reduced activity compared to the wild-type enzyme
V206A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 81% reduced activity compared to the wild-type enzyme
D207N
-
site-directed mutagenesis, inactive mutant
-
K208A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 28% reduced activity compared to the wild-type enzyme
-
N209A
-
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
-
Q118A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, inactive mutant
-
T244A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 65% reduced activity compared to the wild-type enzyme
-
D104A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D104A/E115Q/D245A
site-directed mutagenesis, almost inactive mutant
D104N
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
D104N/D206N/D245N
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D104N/D206N/D245N/E115Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D206A
site-directed mutagenesis, the enzyme activity is modestly reduced compared to wild-type
D206A/D245A
site-directed mutagenesis, the enzyme activity is abolished in the double mutant
D206N
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
D245A
site-directed mutagenesis, the enzyme activity is modestly reduced compared to wild-type
D245N
site-directed mutagenesis, the mutation has no significant effect on the A-preference for TktRNAAsp, but exhibits a modest, but shows about 4fold reduced G-preference activity compared to wild-type
E115Q
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
G202R
site-directed mutagenesis, the mutant is nearly inactive, nearly complete loss of both m1G9 and m1A9 activity
G242R
site-directed mutagenesis, the mutant shows unaltered activity
Q122A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D104A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
D104N
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
-
D206A
-
site-directed mutagenesis, the enzyme activity is modestly reduced compared to wild-type
-
D206N
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
-
E115Q
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
-
additional information
5-fluorouracil (5FU) hypersensitive phenotype of trm10 deletion in Saccharomyces cerevisiae. Growth of the trm10DELTA strain is inhibited compared to a TRM10 wild-type strain in media containing 0.001 mg/ml 5FU. This growth defect is due to the loss of TRM10, since expression of a wild-type copy of either ScTrm10 or hTRMT10A complements this phenotype at either 30 °C or 37°C, while expression of the empty vector does not restore wild-type growth to the trm10DELTA strain. Cells expressing the hTRMT10A D210N variant are similarly resistant to the effects of 5FU as either wild-type enzyme, consistent with the in vitro biochemical results
D210N
site-directed mutagenesis, inactive mutant
D210N
site-directed mutagenesis, the mutant does not abolish the mutant enzyme's activity, but modestly decreases it
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Jackman, J.E.; Montange, R.K.; Malik, H.S.; Phizicky, E.M.
Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9
RNA
9
574-585
2003
Saccharomyces cerevisiae (Q12400), Saccharomyces cerevisiae
brenda
Kempenaers, M.; Roovers, M.; Oudjama, Y.; Tkaczuk, K.L.; Bujnicki, J.M.; Droogmans, L.
New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA
Nucleic Acids Res.
38
6533-6543
2010
Saccharomyces cerevisiae (Q12400), Thermococcus kodakarensis (Q5JD38)
brenda
Shao, Z.; Yan, W.; Peng, J.; Zuo, X.; Zou, Y.; Li, F.; Gong, D.; Ma, R.; Wu, J.; Shi, Y.; Zhang, Z.; Teng, M.; Li, X.; Gong, Q.
Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate
Nucleic Acids Res.
42
509-525
2014
Schizosaccharomyces pombe (O14214), Schizosaccharomyces pombe, Saccharomyces cerevisiae (Q12400), Saccharomyces cerevisiae, Schizosaccharomyces pombe 972 (O14214)
brenda
Igoillo-Esteve, M.; Genin, A.; Lambert, N.; Desir, J.; Pirson, I.; Abdulkarim, B.; Simonis, N.; Drielsma, A.; Marselli, L.; Marchetti, P.; Vanderhaeghen, P.; Eizirik, D.; Wuyts, W.; Julier, C.; Chakera, A.; Ellard, S.; Hattersley, A.; Abramowicz, M.; Cno
tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans
PLoS Genet.
9
e1003888
2013
Homo sapiens (Q8TBZ6), Homo sapiens
brenda
Swinehart, W.E.; Henderson, J.C.; Jackman, J.E.
Unexpected expansion of tRNA substrate recognition by the yeast m1G9 methyltransferase Trm10
RNA
19
1137-1146
2013
Saccharomyces cerevisiae (Q12400), Saccharomyces cerevisiae, Homo sapiens (Q8TBZ6)
brenda
Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Schizosaccharomyces pombe (O14214), Saccharomyces cerevisiae (Q12400), Thermococcus kodakarensis (Q5JD38), Homo sapiens (Q7L0Y3), Homo sapiens (Q8TBZ6), Thermococcus kodakarensis JCM 12380 (Q5JD38), Schizosaccharomyces pombe ATCC 24843 (O14214), Schizosaccharomyces pombe 972 (O14214), Saccharomyces cerevisiae ATCC 204508 (Q12400), Thermococcus kodakarensis ATCC BAA-918 (Q5JD38)
brenda
Krishnamohan, A.; Dodbele, S.; Jackman, J.
Insights into catalytic and tRNA recognition mechanism of the dual-specific tRNA methyltransferase from Thermococcus kodakarensis
Genes (Basel)
10
100
2019
Thermococcus kodakarensis (Q5JD38), Thermococcus kodakarensis
brenda
Krishnamohan, A.; Jackman, J.E.
Mechanistic features of the atypical tRNA m1G9 SPOUT methyltransferase, Trm10
Nucleic Acids Res.
45
9019-9029
2017
Saccharomyces cerevisiae (Q12400), Saccharomyces cerevisiae, Homo sapiens (Q8TBZ6), Saccharomyces cerevisiae ATCC 204508 (Q12400)
brenda
Howell, N.; Jora, M.; Jepson, B.; Limbach, P.; Jackman, J.
Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B
RNA
25
1366-1376
2019
Homo sapiens (Q8TBZ6), Homo sapiens
brenda