Near-cognate Suppression of Amber, Opal and Quadruplet Codons Competes with Aminoacyl-tRNAPyl for Genetic Code Expansion

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2012 Oct 6

PMID 23036644

Citations 44

Authors

Patrick ODonoghue

Laure Prat

Ilka U Heinemann

Jiqiang Ling

Keturah Odoi

Wenshe R Liu

Dieter Soll

Affiliations

Soon will be listed here.

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.

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