Beyond the canonical 20 amino acids: expanding the genetic lexicon

J Biol Chem. 2010 Apr 9;285(15):11039-44. doi: 10.1074/jbc.R109.091306. Epub 2010 Feb 10.

Abstract

The ability to genetically encode unnatural amino acids beyond the common 20 has allowed unprecedented control over the chemical structures of recombinantly expressed proteins. Orthogonal aminoacyl-tRNA synthetase/tRNA pairs have been used together with nonsense, rare, or 4-bp codons to incorporate >50 unnatural amino acids into proteins in Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, and mammalian cell lines. This has allowed the expression of proteins containing amino acids with novel side chains, including fluorophores, post-translational modifications, metal ion chelators, photocaged and photocross-linking moieties, uniquely reactive functional groups, and NMR, IR, and x-ray crystallographic probes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acids / chemistry*
  • Animals
  • Biochemistry / methods*
  • Cell Line
  • Escherichia coli / metabolism
  • Humans
  • Models, Biological
  • Models, Chemical
  • Models, Genetic
  • Pichia / metabolism
  • Protein Processing, Post-Translational
  • RNA, Transfer / metabolism
  • Saccharomyces cerevisiae

Substances

  • Amino Acids
  • RNA, Transfer