EC Number |
General Information |
Reference |
---|
2.1.1.229 | evolution |
comparison of the MnmC2 active sites between Escherichia coli MnmC and Yersinia pestis MnmC, overview. Structural comparison with MnmC2 of Aquifex aeolicus |
-, 735868, 735869 |
2.1.1.229 | evolution |
conservation of Arg199, the key residue of CmoA that stabilizes the negative charge of the carboxyl group of the S-adenosyl-S-carboxymethyl-L-homocysteine cofactor, suggests that these proteins contain the S-adenosyl-S-carboxymethyl-L-homocysteine cofactor instead of S-adenosyl-L-methionine. The equivalent residue in known S-adenosyl-L-methionine-dependent methyltransferases is not conserved |
735357 |
2.1.1.229 | evolution |
the mcm5U family of modifications is found only in eukaryotes and is implicated in efficient reading of AGA and AAG codons by tRNAArg (UCU) and tRNAGlu(UUC), respectively in Saccharomyyces cerevisiae. Trm112 partners with several methyltransferases involved in diverse translational processes and has distinct roles in other methyltransferase complexes |
737223 |
2.1.1.229 | malfunction |
5-methoxycarbonylmethyl-uridine or 5-methoxycarbonylmethyl-2-thiouridine are absent in tRNAs in trm9DELTA or trm112DELTA mutants, while intermediates 5-carbamoylmethyluridine and 5-methoxycarbonylmethyl-2-thiouridine are accumulating |
720827 |
2.1.1.229 | malfunction |
ABH8 depletion in human cells reduces endogenous levels of 5-methoxycarboxymethyluridine in RNA and increases cellular sensitivity to DNA-damaging agents |
713017 |
2.1.1.229 | malfunction |
in intact yeast cells, disruption of the TRM9 gene results in the complete loss of the modified wobble bases (5-methylcarbonylmethyluridine in tRNAArg3 and 5-methylcarbonylmethyl-2-thiouridine in tRNAGlu) and increased sensitivity at 37°C to paromomycin, a translational inhibitor. trm9-deletion mutants are hypersensitive to the translational inhibitor paromomycin at elevated temperatures, suggesting the importance of the methyl-esterified bases during heat shock |
659936 |
2.1.1.229 | malfunction |
mcm5U, mcm5Um, and mcm5s2U are detected in total tRNA from wild-type livers but are completely absent from total tRNA from Alkbh8-/- mice. Substantial amounts of cm5U, the putative unmethylated precursor of mcm5U, is detected in total tRNA from Alkbh8-/- mice but not in total tRNA from wild-type mice. Despite the complete loss of all of these uridine modifications, Alkbh8-/- mice appear normal. However, the selenocysteine-specific tRNA is aberrantly modified in the Alkbh8-/- mice, and for the selenoprotein Gpx1, a reduced recoding of the UGA stop codon to selenocysteine is observed |
713016 |
2.1.1.229 | malfunction |
silencing of ALKBH8 through small interfering RNA transfection reduced reactive oxygen species (ROS) production via down-regulation of NAD(P)H oxidase-1 (NOX-1) and induced apoptosis through subsequent activation of c-jun NH2-terminal kinase (JNK) and p38. Silencing of ALKBH8 significantly suppresses invasion, angiogenesis, and growth of bladder cancers in vivo |
711667 |
2.1.1.229 | malfunction |
trm9DELTA cells lacking a tRNA methylase specific for wobble uridine (U34) residues survive zymocin |
713048 |
2.1.1.229 | malfunction |
Trm9DELTA mutation causes lack of the 5-methoxycarbonylmethyluridine (mcm5U34) modification in yeast which is associated with sensitivity to DNA damaging agents as well as with sensitivity to aminoglycosides at high temperature and resistance to zymocin-mediated tRNA cleavage and cell death. Mutants encoding Sc Trm9 variants lacking the C-terminal domain required for interaction with Sc Trm112 act as suppressors of zymocin toxicity |
737223 |