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Dynamics of Protein Complexes
Author(s) -
Washburn Michael
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.70.1
Subject(s) - proteomics , context (archaeology) , quantitative proteomics , computational biology , histone , chromatin remodeling , histone deacetylase , chromatin , posttranslational modification , chemistry , multiprotein complex , biology , acetylation , microbiology and biotechnology , biochemistry , dna , enzyme , paleontology , gene
Protein complexes may change their stoichiometry, content, or modifications based on stimuli like changes in the cell cycle or due to a drug treatment. In addition, depending on which protein in a complex is used as a bait protein for affinity purification, different forms of a protein complex may be detected and identified. These changes in complex content and form have functional implications. Carrying out studies regarding the dynamics of protein complexes has required the development of advanced quantitative proteomics technologies. We have refined the proteomics approach named multidimensional protein identification technology (MudPIT) and developed the label free quantitative proteomics approach termed the normalized spectral abundance factor (NSAF) for the analysis of multiprotein complexes. With a primary focus on transcriptional regulatory complexes, we have applied these approaches to the study of the Rpd3 histone deacetylase chromatin remodeling complexes, Mediator, and RNA Polymerase II. This presentation will describe the technology we use to characterize these complexes and will demonstrate the changes in these complexes that occur depending on the cellular context.