![]() ![]() When expressed as a Gal4 fusion protein, CIR repressed reporter gene expression. Two CBF1 mutants that were unable to bind CIR did not function as repressors, suggesting that targeting of CIR to CBF1 is an important component of repression. A CIR homolog is encoded by Caenorhabditis elegans, indicating that CIR is evolutionarily conserved. We have examined the mechanism of CBF1-mediated repression and show that CBF1 binds to a unique corepressor, CBF1 interacting corepressor (CIR). The Epstein–Barr virus-immortalizing protein EBNA2 activates both cellular and viral gene expression by targeting CBF1 and mimicking NotchIC. Notch is a transmembrane protein involved in cell-fate decisions, and the cytoplasmic domain of Notch (NotchIC) targets CBF1. CSL proteins play a central role in Notch signaling and in Epstein–Barr virus-induced immortalization. ![]() CBF1 is a member of the CSL family of DNA binding factors, which mediate either transcriptional repression or transcriptional activation. ![]()
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