A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli

Mol Biosyst. 2010 Apr;6(4):683-6. doi: 10.1039/b920120c. Epub 2010 Feb 15.

Abstract

By overexpressing the C-terminal domain of the ribosomal protein L11 to decrease release factor 1-mediated termination of protein translation, enhanced amber suppression is achieved in E. coli. This enhanced amber suppression efficiency allows the genetic incorporation of three N(epsilon)-acetyl-l-lysines into one GFP(UV) protein in E. coli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Amino Acids / metabolism*
  • Base Sequence
  • Codon, Terminator
  • DNA, Bacterial / genetics
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism*
  • Genes, Bacterial
  • Green Fluorescent Proteins / chemistry
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Lysine / analogs & derivatives
  • Lysine / chemistry
  • Lysine / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Processing, Post-Translational
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / genetics
  • Ribosomal Proteins / metabolism
  • Spectrometry, Mass, Electrospray Ionization
  • Systems Biology

Substances

  • Amino Acids
  • Codon, Terminator
  • DNA, Bacterial
  • Escherichia coli Proteins
  • Recombinant Fusion Proteins
  • Ribosomal Proteins
  • ribosomal protein L11
  • Green Fluorescent Proteins
  • N-epsilon-acetyllysine
  • Lysine