Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.

Abstract

Over 300 amino acids are found in proteins in nature, yet typically only 20 are genetically encoded. Reassigning stop codons and use of quadruplet codons emerged as the main avenues for genetically encoding non-canonical amino acids (NCAAs). Canonical aminoacyl-tRNAs with near-cognate anticodons also read these codons to some extent. This background suppression leads to 'statistical protein' that contains some natural amino acid(s) at a site intended for NCAA. We characterize near-cognate suppression of amber, opal and a quadruplet codon in common Escherichia coli laboratory strains and find that the PylRS/tRNA(Pyl) orthogonal pair cannot completely outcompete contamination by natural amino acids.

DOI: 10.1016/j.febslet.2012.09.033
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@article{ODonoghue2012NearcognateSO, title={Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.}, author={Patrick O'Donoghue and Laure Prat and Ilka U Heinemann and Jiqiang Ling and Keturah Odoi and Wenshe R Liu and Dieter S{\"{o}ll}, journal={FEBS letters}, year={2012}, volume={586 21}, pages={3931-7} }