EC Number   |
General Information |
Reference |
|---|
   2.1.1.33 | evolution |
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 |
737060 |
| 2.1.1.33 | malfunction |
absence of m7G46 results in temperature-sensitive growth |
675921 |
| 2.1.1.33 | malfunction |
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 |
737060 |
| 2.1.1.33 | malfunction |
protein synthesis in DELTAtrmB cells is depressed above 70°C. At 80°C, the DtrmB strain exhibits a severe growth defect |
705989 |
| 2.1.1.33 | 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 |
676233 |
| 2.1.1.33 | physiological function |
m7G46 methyltransferase Trm8p/Trm82p acts as a hub of synthetic interactions with several tRNA modification enzymes, resulting in temperature-sensitive growth |
675921 |
| 2.1.1.33 | physiological function |
N7 cap methylation is essential for viral replication |
705423 |
| 2.1.1.33 | physiological function |
N7-MTase plays an important role in SARS-coronavirus replication/transcription |
706535 |
| 2.1.1.33 | physiological function |
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 |
737060 |
| 2.1.1.33 | 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 |
757114 |
