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/tRNAPyl orthogonal pair cannot completely outcompete contamination by natural amino acids.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Oct 01, 2012
- Source ID
- 10.1016/j.febslet.2012.09.033
Entities
People
- Dieter Söll
- Ilka U. Heinemann
- Jiqiang Ling
- Keturah Odoi
- Laure Prat
- Patrick O’donoghue
- Wenshe R. Liu
Organizations
- Defense Advanced Research Projects Agency
- National Institutes of Health
- Robert A. Welch Foundation