Periodate-Triggered Cross-Linking of DOPA-Containing Peptide−Protein Complexes

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 un...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2004-09, Vol.126 (37), p.11442-11443
Main Authors: Burdine, Lyle, Gillette, Thomas G, Lin, Hai-Jun, Kodadek, Thomas
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cross-Linking Reagents - chemistry
Dihydroxyphenylalanine - chemistry
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Molecular Sequence Data
Oxidation-Reduction
Peptides - chemistry
Periodic Acid - chemistry
Proteins
Quinones - chemistry
Repressor Proteins - analysis
Repressor Proteins - chemistry
Saccharomyces cerevisiae Proteins - analysis
Saccharomyces cerevisiae Proteins - chemistry
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja045982c