Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.

@article{Hati2006PretransferEB,
  title={Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.},
  author={Sanchita Hati and Brigitte K Ziervogel and Julius Sternjohn and Fai-Chu Wong and Maria C. Nagan and Abbey E. Rosen and Paul G. Siliciano and Joseph W Chihade and Karin Musier-Forsyth},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 38},
  pages={27862-72}
}
Aminoacyl-tRNA synthetases catalyze the attachment of cognate amino acids to specific tRNA molecules. To prevent potential errors in protein synthesis caused by misactivation of noncognate amino acids, some synthetases have evolved editing mechanisms to hydrolyze misactivated amino acids (pre-transfer editing) or misacylated tRNAs (post-transfer editing). In the case of post-transfer editing, synthetases employ a separate editing domain that is distinct from the site of amino acid activation… CONTINUE READING