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Periodate-triggered cross-linking of dopa-containing peptide-protein complexes

Academic Article
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Overview

authors

  • Burdine, L.
  • Gillette, T. G.
  • Lin, H. J.
  • Kodadek, Thomas

publication date

  • September 2004

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Chemical cross-linking is a powerful methodology for analyzing proteins-small molecule and protein-protein interactions. We describe the development of a new chemical cross-linking reaction for the study of protein complexes. Specifically, we show that molecules containing an ortho dihydroxyarene unit can be oxidized selectively with sodium periodate in the presence of native proteins, producing an ortho quinone intermediate that can cross-link with suitable nearby protein residues. We demonstrate the efficacy and specificity of this chemistry for a peptide-protein complex and also deduce the binding site of an artificial activation domain on a proteasome subcomplex.

subject areas

  • Amino Acid Sequence
  • Cross-Linking Reagents
  • Dihydroxyphenylalanine
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Peptides
  • Periodic Acid
  • Quinones
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja045982c

PubMed ID

  • 15366882
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Additional Document Info

start page

  • 11442

end page

  • 11443

volume

  • 126

issue

  • 37

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