Hyperactive Editing Domain Variants Switch the Stereospecificity of Tyrosyl-tRNA Synthetase.

@article{Richardson2016HyperactiveED,
  title={Hyperactive Editing Domain Variants Switch the Stereospecificity of Tyrosyl-tRNA Synthetase.},
  author={Charles Joseph Richardson and Eric A. First},
  journal={Biochemistry},
  year={2016},
  volume={55 17},
  pages={2526-37}
}
d-Amino acids are excluded at three different steps during protein synthesis: the aminoacylation of tRNA, binding of aminoacyl-tRNAs to EF-Tu, and selection of the aminoacyl-tRNA by the ribosome. We previously altered the enantioselectivity of tyrosyl-tRNA synthetase (TyrRS) by inserting the editing domain from phenylalanyl-tRNA synthetase (FRSed) between Gly 161 and Ile 162 in tyrosyl-tRNA synthetase (the editing domain hydrolyzes l-Tyr-tRNA but not d-Tyr-tRNA). In this paper, we test the… CONTINUE READING
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