Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics
Copyright policy )Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics
AbstractTo discriminate between stable and dynamic protein–protein interactions, we propose a strategy in which cells with and without tagged bait are differentially labeled with stable isotope and combined prior to complex purification. Mass‐spectrometric analysis of the purified complexes identifies stable and dynamic components as those derived exclusively from the tagged cells and those from both cells, respectively. We successfully applied this strategy to analyze two yeast protein complexes, eIF2B–eIF2 and cyclin–Cdc28.
- University of Tokyo Japan
Proteomics, Saccharomyces cerevisiae Proteins, Eukaryotic Initiation Factor-2, Reproducibility of Results, Models, Biological, Mass Spectrometry, Eukaryotic Initiation Factor-2B, Protein Subunits, Tandem Mass Spectrometry, Cyclins, Isotope Labeling, CDC28 Protein Kinase, S cerevisiae, Chromatography, Liquid, Protein Binding
Proteomics, Saccharomyces cerevisiae Proteins, Eukaryotic Initiation Factor-2, Reproducibility of Results, Models, Biological, Mass Spectrometry, Eukaryotic Initiation Factor-2B, Protein Subunits, Tandem Mass Spectrometry, Cyclins, Isotope Labeling, CDC28 Protein Kinase, S cerevisiae, Chromatography, Liquid, Protein Binding
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