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Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid

Academic Article
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Overview

related to degree

  • Lee, Hyun Soo, Ph.D. in Chemistry, Scripps Research 2005 - 2009

authors

  • Lee, Hyun Soo
  • Dimla, R. D.
  • Schultz, Peter

publication date

  • September 2009

journal

  • Bioorganic & Medicinal Chemistry Letters  Journal

abstract

  • The photo-crosslinking amino acid, p-benzoyl-L-phenylalanine (pBpa), was genetically incorporated into Escherichia coli catabolite activator protein (CAP) in bacteria in response to an amber nonsense codon using an orthogonal tRNA/aminoacyl-tRNA synthetase pair. The mutant CAP (CAP-K26Bpa) containing pBpa formed a covalent complex with a DNA fragment containing the consensus operator sequence upon UV irradiation. Because this amino acid can be genetically incorporated into any DNA-binding protein in E. coli, yeast or mammalian cells with minimal perturbation of protein structure, this method should be generally useful for investigating DNA-protein interactions.

subject areas

  • Amino Acids
  • Amino Acyl-tRNA Synthetases
  • Base Sequence
  • Benzophenones
  • Cross-Linking Reagents
  • Cyclic AMP Receptor Protein
  • DNA
  • Escherichia coli
  • Molecular Sequence Data
  • Protein Binding
  • RNA, Transfer
  • Ultraviolet Rays
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Research

keywords

  • Benzophenone
  • Photo-crosslinking
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Identity

PubMed Central ID

  • PMC2873854

International Standard Serial Number (ISSN)

  • 0960-894X

Digital Object Identifier (DOI)

  • 10.1016/j.bmcl.2009.07.011

PubMed ID

  • 19643606
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Additional Document Info

start page

  • 5222

end page

  • 5224

volume

  • 19

issue

  • 17

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