2.1.1.33: tRNA (guanine46-N7)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanine46-N7)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.33
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2.1.1.33
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methyltransferase-like
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n7-methylguanosine
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cyp27b1
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mettl21b
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trnaphe
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mescs
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kidney-specific
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methylome
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submodules
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methyl-transfer
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pharmacology
- 2.1.1.33
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methyltransferase-like
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n7-methylguanosine
- cyp27b1
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mettl21b
- trnaphe
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mescs
-
kidney-specific
-
methylome
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submodules
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methyl-transfer
- pharmacology
Reaction
Synonyms
7-methylguanine transfer ribonucleate methylase, m7G-methyltransferase, m7G46 methyltransferase Trm8p/Trm82p, methyltransferase like 1, methyltransferase, transfer ribonucleate guanine 7-, METTL1, N7-methylguanine methylase, PA14_05000, transfer ribonucleate guanine 7-methyltransferase, transfer RNA (m7G46) methyltransferase, Trm8–Trm82 complex, TrmB, TrMet (m7G46), tRNA (m7G46) methyltransferase, tRNA guanine 7-methyltransferase
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General Information
General Information on EC 2.1.1.33 - tRNA (guanine46-N7)-methyltransferase
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evolution
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nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature tRNA molecules and prevent rapid tRNA decay. The tRNA modifying enzymes, NSUN2 and METTL1, are mammalian orthologues of yeast Trm4 and Trm8, which are required for protecting tRNA against tRNA decay
malfunction
physiological function
Q03774; Q12009
absence of m7G46 results in temperature-sensitive growth
malfunction
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protein synthesis in DELTAtrmB cells is depressed above 70°C. At 80°C, the DtrmB strain exhibits a severe growth defect
malfunction
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combined knockdown of NSUN2, EC 2.1.1.203, and METTL1 in HeLa cells drastically potentiate sensitivity of cells to 5-fluorouracil, but does not affect cisplatin- and paclitaxel-induced cytotoxicity, synergistic effects of NSUN2 and METTL1 double knockdown, which causes rapid tRNA(ValAAC) degradation induced by destabilizing 5-fluorouracil
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N7 cap methylation is essential for viral replication
physiological function
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N7-MTase plays an important role in SARS-coronavirus replication/transcription
physiological function
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the m7G46 modification catalyzed by TrmB may act as one of the key factors in tRNA modification network
physiological function
long C-terminal region of the thermophilic TrmB protein is involved in the protein stability but does not function in the RNA recognition
physiological function
Q03774; Q12009
m7G46 methyltransferase Trm8p/Trm82p acts as a hub of synthetic interactions with several tRNA modification enzymes, resulting in temperature-sensitive growth
physiological function
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the m7G46 modification is required for cell viability at high temperatures via a tRNA modification network. The m7G46 modification induces nearly full modification of several modified nucleotides such as Gm18 and m1G37
physiological function
Q03774; Q12009
Trm8p is required for m7G modification. Trm82p is required to maintain cellular levels of Trm8p and to stabilize Trm8p in an active conformation
physiological function
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Nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature tRNA molecules and prevent rapid tRNA decay. The tRNA modifying enzyme METTL1 is a mammalian orthologues of yeast Trm8, which is required for protecting tRNA against tRNA decay
physiological function
residues Glu47, Tyr95, Arg108, Thr165 and Tyr167 residues are important for AdoMet binding and Asp74, Asp97, and Thr132 are important for the methyltransfer reaction. During the reaction, the carboxyl group in Asp133 captures the proton of N-H in the guanine base. Thr132 may assist the interaction by formation of a hydrogen bond between the OH group in Thr132 and the O6 atom in the guanine base. Interactions between Thr132, Asp133 and tRNA decide the direction of the guanine base and the N7 atom in G46 causes the nucleophilic attack against the activated methyl group in the bound AdoMet
physiological function
the abundance of m7G in the tRNA extracted from trmB complemented strain is about 50% lower than the abundance of m7G extracted from the wild type strain. Pseudomonas aeruginosa shows a tRNA modification-mediated translational response to H2O2. Loss of TrmB has a strong negative effect on the translation of Phe- and Asp-enriched mRNAs. The TrmB-mediated m7G modification modulates the expression of the catalase genes KatA and KatB, which are enriched with Phe/Asp codons at the translational level. In response to H2O2 exposure, the level of m7G modification increases, consistent with the increased translation efficiency of Phe- and Asp-enriched mRNAs. Inactivation of TrmB leads to decreased KatA and KatB protein abundance and decreased catalase activity, resulting in H2O2-sensitive phenotype
physiological function
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the abundance of m7G in the tRNA extracted from trmB complemented strain is about 50% lower than the abundance of m7G extracted from the wild type strain. Pseudomonas aeruginosa shows a tRNA modification-mediated translational response to H2O2. Loss of TrmB has a strong negative effect on the translation of Phe- and Asp-enriched mRNAs. The TrmB-mediated m7G modification modulates the expression of the catalase genes KatA and KatB, which are enriched with Phe/Asp codons at the translational level. In response to H2O2 exposure, the level of m7G modification increases, consistent with the increased translation efficiency of Phe- and Asp-enriched mRNAs. Inactivation of TrmB leads to decreased KatA and KatB protein abundance and decreased catalase activity, resulting in H2O2-sensitive phenotype
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