Genetic introduction of a diketone-containing amino acid into proteins

Bioorg Med Chem Lett. 2006 Oct 15;16(20):5356-9. doi: 10.1016/j.bmcl.2006.07.094. Epub 2006 Aug 24.

Abstract

An orthogonal tRNA/aminoacyl-tRNA synthetase pair was evolved that makes possible the site-specific incorporation of an unnatural amino acid bearing a beta-diketone side chain into proteins in Escherichia coli with high translational efficiency and fidelity. Proteins containing this unnatural amino acid can be efficiently and selectively modified with hydroxylamine derivatives of fluorophores and other biophysical probes.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acids / chemistry*
  • Amino Acyl-tRNA Synthetases / chemistry
  • Binding Sites
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Ketones / chemistry*
  • Molecular Conformation
  • Mutagenesis, Site-Directed / methods*
  • Protein Engineering / methods
  • Proteins / chemistry*
  • Proteins / genetics*
  • RNA, Transfer / chemistry
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Amino Acids
  • Ketones
  • Proteins
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases