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Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli

Academic Article
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Overview

authors

  • Chin, J. W.
  • Martin, A. B.
  • King, D. S.
  • Wang, L.
  • Schultz, Peter

publication date

  • August 2002

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Benzophenones are among the most useful photocrosslinking agents in biology. We have evolved an orthogonal aminoacyl-tRNA synthetase/tRNA pair that makes possible the in vivo incorporation of p-benzoyl-l-phenylalanine into proteins in Escherichia coli in response to the amber codon, TAG. This unnatural amino acid was incorporated with high translational efficiency and fidelity into the dimeric protein glutathione S-transferase. Irradiation resulted in efficient crosslinking (>50%) of the protein subunits. This methodology may prove useful for discovering and defining protein interactions in vitro and in vivo.

subject areas

  • Amino Acids
  • Amino Acyl-tRNA Synthetases
  • Cloning, Molecular
  • Cross-Linking Reagents
  • Escherichia coli
  • Genetic Code
  • Green Fluorescent Proteins
  • Luminescent Proteins
  • Models, Molecular
  • Protein Conformation
  • Tyrosine-tRNA Ligase
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Identity

PubMed Central ID

  • PMC123203

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.172226299

PubMed ID

  • 12154230
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Additional Document Info

start page

  • 11020

end page

  • 11024

volume

  • 99

issue

  • 17

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