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

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.

authors

• Liu, Wenshe

published proceedings

• FEBS Lett

altmetric score

• 9

author list (cited authors)

• O'Donoghue, P., Prat, L., Heinemann, I. U., Ling, J., Odoi, K., Liu, W. R., & Sll, D.

citation count

• 62

complete list of authors

• O'Donoghue, Patrick||Prat, Laure||Heinemann, Ilka U||Ling, Jiqiang||Odoi, Keturah||Liu, Wenshe R||Söll, Dieter

publication date

• November 2012

publisher

• Wiley  Publisher

published in

• FEBS Letters  Journal

keywords

• Anticodon
• Codon
• Escherichia Coli
• Genetic Code
• Lysine
• Protein Biosynthesis
• Rna, Transfer, Amino Acyl
• Spectrometry, Mass, Electrospray Ionization
• Suppression, Genetic

PubMed Central ID

• 23036644

Digital Object Identifier (DOI)

• 10.1016/j.febslet.2012.09.033

start page

• 3931

end page

• 3937

volume

• 586

issue

• 21

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.febslet.2012.09.033