ORGN 673 |
| Gene-specific transcription relies on transcriptional activator proteins to recruit an array of proteins constituting the transcriptional machinery to binding sites proximal to a gene in order to initiate gene transcription. However, the functional relevance of specific activator protein-transcriptional machinery contacts remains largely unknown. Recently, Tra1 a component of the yeast SAGA and NuA4 complexes has been shown to be a target of the Gal4, GCN4 and VP16 activation domains (ADs). To identify this binding surface, we have expressed various fragments of Tra1 in E. coli. Using fluorescence polarization-based binding assays, we have found a C-terminal region to be important for interaction with transcriptional activators. To probe the role of this interaction in activation, a combinatorial library is being screened to isolate ligands that bind the C-terminus of Tra1. Further, combinations of these ligands with Med15-specific ADs, will be used to investigate the mechanism of synergistic activation by simultaneously targeting proteins in different transcription complexes.
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Organic Chemistry |
