Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions

@inproceedings{Moukadiri2009EvolutionarilyCP,
  title={Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions},
  author={Isma{\"i}l Moukadiri and Silvia Regina Tozato Prado and Julio Piera and Adri{\'a}n Vel{\'a}zquez-Campoy and Glenn R. Bj{\"o}rk and M.-Eugenia Armengod},
  booktitle={Nucleic acids research},
  year={2009}
}
The wobble uridine of certain bacterial and mitochondrial tRNAs is modified, at position 5, through an unknown reaction pathway that utilizes the evolutionarily conserved MnmE and GidA proteins. The resulting modification (a methyluridine derivative) plays a critical role in decoding NNG/A codons and reading frame maintenance during mRNA translation. The lack of this tRNA modification produces a pleiotropic phenotype in bacteria and has been associated with mitochondrial encephalomyopathies in… CONTINUE READING

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