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Papers In Press, published online ahead of print September 15, 2002
Radiaton Oncology, New England Medical Center, Tufts University School of Medicine, Boston, MA 02111
Corresponding Author: vband{at}lifespan.org
The expression of human papillomavirus (HPV) E6 oncoprotein is causally linked to high-risk HPV associated human cancers. We have recently isolated hADA3, the human homologue of yeast transcriptional co-activator yADA3, as a novel E6 target. Human ADA3 binds to the high-risk (cancer-associated) but not the low-risk HPV E6 proteins, and to immortalization-competent but not to immortalization-defective HPV16 E6 mutants, suggesting a role for the perturbation of hADA3 function in E6-mediated oncogenesis. We demonstrate here that hADA3 directly binds to RXR alpha in vitro and in vivo. Using chromatin immunoprecipitation, we show that hADA3 is part of activator complexes bound to the native RXR-response elements within the promoter of the cyclin-dependent kinase inhibitor gene p21. We show that hADA3 enhances the RXR alpha-mediated sequence-specific transactivation of retinoid target genes, cellular retinoic acid-binding protein II and p21. Significantly, we demonstrate that E6 inhibits the RXR alpha-mediated transactivation of target genes, implying that perturbation of RXR-mediated transactivation by E6 could contribute to HPV oncogenesis.
J. Biol. Chem, 10.1074/jbc.M208447200
Submitted on August 19, 2002
Revised on September 10, 2002
Accepted on September 15, 2002
Human papilloma virus 16 E6 oncoprotein inhibits RXR-mediated transactivation by targeting human ADA3 coactivator
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