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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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December 20, 2010
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Capture Compounds are trifunctional small molecules to reduce the complexity of the proteome by functional reversible small molecule-protein interaction followed by photo-crosslinking and purification. Here we use a Capture Compound with S-adenosyl-L-homocysteine-binding as selectivity function to isolate methyltransferases from an Escherichia coli whole cell lysate and identify them by MS.
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MethyltransferasesS-adenosyl-L-homocysteine-binding ProteinsCapture Compound Mass SpectrometryAffinity ChromatographyActivity-based Protein ProfilingTrifunctional Capture CompoundsPhoto-crosslinkingSmall Molecule-protein InteractionsSelectivity FunctionSAHSorting FunctionBiotinSolid PhaseStreptavidin Magnetic BeadsOff-bead ConfigurationOn-bead ConfigurationSmall Molecule Of InterestSAMSAM-dependent MethyltransferasesDNA Methylation
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Lenz, T., Poot, P., Gräbner, O., Glinski, M., Weinhold, E., Dreger, M., Köster, H. Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS). J. Vis. Exp. (46), e2264, doi:10.3791/2264 (2010).
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