Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors |
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Authors: | Florens Laurence Carozza Michael J Swanson Selene K Fournier Marjorie Coleman Michael K Workman Jerry L Washburn Michael P |
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Institution: | Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, MO 64110, USA. |
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Abstract: | Mass spectrometry-based approaches are commonly used to identify proteins from multiprotein complexes, typically with the goal of identifying new complex members or identifying post-translational modifications. However, with the recent demonstration that spectral counting is a powerful quantitative proteomic approach, the analysis of multiprotein complexes by mass spectrometry can be reconsidered in certain cases. Using the chromatography-based approach named multidimensional protein identification technology, multiprotein complexes may be analyzed quantitatively using the normalized spectral abundance factor that allows comparison of multiple independent analyses of samples. This study describes an approach to visualize multiprotein complex datasets that provides structure function information that is superior to tabular lists of data. In this method review, we describe a reanalysis of the Rpd3/Sin3 small and large histone deacetylase complexes previously described in a tabular form to demonstrate the normalized spectral abundance factor approach. |
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Keywords: | Chromatin remodeling Protein complexes Multidimensional protein identification technology (MudPIT) Tandem mass spectrometry Normalized spectral abundance factor |
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