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Identification of protein complexes with quantitative proteomics in S. cerevisiae
Published on: March 4, 2009
Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits
K K Lee1, P Prochasson, L Florens
1Stowers Institute for Medical Research, 1000 E. 50th Kansas City, MO 64110, USA.
Abstract:
Epigenetics is the alteration of phenotype without affecting the genotype. An underlying molecular mechanism of epigenetics is the changes of chromatin structure by covalent histone modifications and nucleosome reorganization. In the yeast, Saccharomyces cerevisiae, two of the most well-studied macromolecular complexes that perform these epigenetic changes are the ATP-dependent Swi/Snf chromatin-remodelling complex and the SAGA histone acetyltransferase complex. To understand fully the mechanism by which these large protein complexes perform their functions in the cell, it is crucial that all the subunits of these complexes are identified. In an attempt to identify new subunits associated with SAGA and Swi/Snf, we used tandem affinity purification, followed by a multidimensional protein identification technology to analyse the subunit composition. Our analysis identified two novel proteins, one associated with SAGA, YPL047W (Sgf11), and another associated with Swi/Snf, Rtt102.

