Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain.
Copyright policy )Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain.
Scaffold attachment factor-B1 (SAFB1) is a nuclear matrix protein that has been proposed to couple chromatin structure, transcription, and RNA processing. We have previously shown that SAFB1 can repress estrogen receptor (ERalpha)-mediated transactivation. Here we present a structure-function study showing that transactivation is mediated via an intrinsic and transferable C-terminal repression domain (RD). A similar C-terminal RD was found in the family member SAFB2. Removal of the RD from SAFB1 resulted in a dominant-negative SAFB1 protein that increased ligand-dependent and -independent ERalpha activity. SAFB1RD-mediated repression was partly blocked by histone deacetylase inhibitors; however, no histone deacetylase inhibitors were identified in a yeast two-hybrid screen using the RD as bait. Instead, SAFB1RD was found to interact with TAFII68, a member of the basal transcription machinery. We propose a model in which SAFB1 represses ERalpha activity via indirect association with histone deacetylation and interaction with the basal transcription machinery.
- Baylor College of Medicine United States
- Dignity Health United States
- Indiana University – Purdue University Indianapolis United States
- Indiana University Health United States
- Methodist Hospital United States
Models, Genetic, Genetic Vectors, Immunoblotting, Matrix Attachment Region Binding Proteins, Ligands, Cell Line, Histone Deacetylase Inhibitors, Histones, Mice, Nuclear Matrix-Associated Proteins, Cell Line, Tumor, NIH 3T3 Cells, Animals, Humans, Enzyme Inhibitors, Luciferases, Genes, Dominant, HeLa Cells, Plasmids, Protein Binding
Models, Genetic, Genetic Vectors, Immunoblotting, Matrix Attachment Region Binding Proteins, Ligands, Cell Line, Histone Deacetylase Inhibitors, Histones, Mice, Nuclear Matrix-Associated Proteins, Cell Line, Tumor, NIH 3T3 Cells, Animals, Humans, Enzyme Inhibitors, Luciferases, Genes, Dominant, HeLa Cells, Plasmids, Protein Binding
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