Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain.

@article{Sternjohn2007RestoringSP,
  title={Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain.},
  author={Julius Sternjohn and Sanchita Hati and Paul G. Siliciano and Karin Musier-Forsyth},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 7},
  pages={
          2127-32
        }
}
Aminoacyl-tRNA synthetases are multidomain proteins responsible for the attachment of specific amino acids to their tRNA substrates. Prolyl-tRNA synthetases (ProRSs) are notable due to their particularly diverse architectures through evolution. For example, Saccharomyces cerevisiae ProRS possesses an N-terminal extension with weak homology to a bacterial-specific domain typically present as an insertion (INS) within the aminoacylation active site. The INS domain has been shown to contain a… CONTINUE READING

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