Proceedings of the National Academy of Sciences · 1999 · 577 citations · 32 references
Life SciencesBiochemistryMolecular BiologyProtein BiochemistryProtein-protein InteractionsStructural BiologyMacromolecular AssemblyPhotochemistryProtein ChemistryProtein Complex AnalysisProtein DesignProtein StructureBifunctional LinkersBiomolecule CrosslinkingChemical Cross-linkingCross-linkingOxidant ChemistryPhotolysisProtein CrosslinkingProtein Destabilization
Chemical cross-linking is a potentially useful technique for probing the architecture of multiprotein complexes. However, analyses using typical bifunctional cross-linkers often suffer from poor yields, and large-scale modification of nucleophilic side chains can result in artifactual results attributable to structural destabilization. We report here the de novo design and development of a type of protein cross-linking reaction that uses a photogenerated oxidant to mediate rapid and efficient cross-linking of associated proteins. The process involves brief photolysis of tris-bipyridylruthenium(II) dication with visible light in the presence of the electron acceptor ammonium persulfate and the proteins of interest. Very high yields of cross-linked products can be obtained with irradiation times of <1 second. This chemistry obviates many of the problems associated with standard cross-linking reagents.
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The carboxy-terminal 30 amino acids of GAL4 are recognized by GAL80
Jun Ma, Mark Ptashne · Cell · 1987 · 353 citations