Abstract
RORγ is a nuclear receptor that binds to DNA motifs as a monomer to constitutively activate target genes. RORγ plays an important role in thymocyte development and lymph node organogenesis, while the regulation of RORγ-mediated transcriptional activation is currently unclear. The purpose of this study was to identify other nuclear proteins that interact with RORγ. A yeast two-hybrid screen with Y190 yeast cells under stringent conditions resulted in the identification of CHD4, also known as Mi-2β, as a RORγ-interacting protein. This interaction was confirmed by GST pull-down assays. This interaction occurred within the middle regulatory region (amino acids 719–1164) of Mi-2β. Transfection of Gal4-RORγ into HeLa cells resulted in constitutive transactivation of the MH100-tk-luc reporter. The addition of Mi-2β resulted in a dramatic 50% decrease in Gal4-RORγ-mediated transactivation. These data demonstrate that RORγ forms a protein–protein interaction with the regulatory region of Mi-2β, resulting in inhibition of RORγ transcriptional activity. These results may provide evidence as to how RORγ-mediated transactivation is regulated by other nuclear proteins.
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