Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion. O’Donoghue, P., Prat, L., Heinemann, I. U., Ling, J., Odoi, K., Liu, W. R., & Söll, D. FEBS Letters, 586(21):3931–3937, November, 2012. ![Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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/tRNAPyl orthogonal pair cannot completely outcompete contamination by natural amino acids.
@article{odonoghue_near-cognate_2012,
title = {Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-{tRNAPyl} for genetic code expansion},
volume = {586},
issn = {0014-5793},
url = {https://www.sciencedirect.com/science/article/pii/S0014579312007417},
doi = {10.1016/j.febslet.2012.09.033},
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/tRNAPyl orthogonal pair cannot completely outcompete contamination by natural amino acids.},
language = {en},
number = {21},
urldate = {2021-11-24},
journal = {FEBS Letters},
author = {O’Donoghue, Patrick and Prat, Laure and Heinemann, Ilka U. and Ling, Jiqiang and Odoi, Keturah and Liu, Wenshe R. and Söll, Dieter},
month = nov,
year = {2012},
keywords = {4-Base codon, Boc-lysine, Orthogonal translation systems, Pyrrolysyl-tRNA synthetase, Synthetic biology, tRNA},
pages = {3931--3937},
}
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