Functional interaction between the p160 coactivator proteins and the transcriptional enhancer factor family of transcription factors.

SRC1, initially identified as a nuclear receptor coactivator, was found to interact with a member of the transcriptional enhancer factor (TEF) family of transcription factors, TEF-4. The interaction, which occurs in both intact cells and in a cell-free system, is mediated by the highly conserved basic helix-loop-helix/Per-Arnt-Sim (bHLH-PAS) domain present ...
in the N-terminal region of SRC1. Moreover, all three members of the p160 family of nuclear receptor coactivators, SRC1, TIF2, and RAC3, are able to potentiate transcription from a TEF response element in transient transfection experiments, and this activation requires the presence of the bHLH-PAS domain. These results suggest that the p160 proteins could be bona fide coactivators of the TEF family of transcription factors.
Mesh Terms:
Animals, COS Cells, Cell-Free System, DNA, Complementary, DNA-Binding Proteins, Gene Library, Glutathione Transferase, Hela Cells, Histone Acetyltransferases, Humans, Immunoblotting, Mice, Models, Genetic, Muscle, Skeletal, Myocardium, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 2, Nuclear Receptor Coactivator 3, Plasmids, Protein Structure, Tertiary, Response Elements, Saccharomyces cerevisiae, Trans-Activators, Transcription Factors, Transcription, Genetic, Transfection, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Oct. 06, 2000
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