Mutational separation of two pathways for editing by a class I tRNA synthetase.

  title={Mutational separation of two pathways for editing by a class I tRNA synthetase.},
  author={Tamara L. Hendrickson and Tyzoon K. Nomanbhoy and Val{\'e}rie de Cr{\'e}cy-Lagard and Shuya Fukai and Osamu Nureki and Shigeyuki Yokoyama and Paul R. Schimmel},
  journal={Molecular cell},
  volume={9 2},
Aminoacyl tRNA synthetases (aaRSs) catalyze the first step in protein biosynthesis, establishing a connection between codons and amino acids. To maintain accuracy, aaRSs have evolved a second active site that eliminates noncognate amino acids. Isoleucyl tRNA synthetase edits valine by two tRNA(Ile)-dependent pathways: hydrolysis of valyl adenylate (Val-AMP, pretransfer editing) and hydrolysis of mischarged Val-tRNA(Ile) (posttransfer editing). Not understood is how a single editing site… CONTINUE READING


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