The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation.

@article{Sabina2006TheRP,
  title={The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation.},
  author={Jeffrey Sabina and Dieter S{\"o}ll},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 11},
  pages={6993-7001}
}
Bacterial tRNA-guanine transglycosylase (TGT) replaces the G in position 34 of tRNA with preQ(1), the precursor to the modified nucleoside queuosine. Archaeal TGT, in contrast, substitutes preQ(0) for the G in position 15 of tRNA as the first step in archaeosine formation. The archaeal enzyme is about 60% larger than the bacterial protein; a carboxyl-terminal extension of 230 amino acids contains the PUA domain known to contact the four 3'-terminal nucleotides of tRNA. Here we show that the C… CONTINUE READING

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