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Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53

Laboratory for Papillomavirus Biology, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Republic of Singapore¹
Institut für Virologie der Universität zu Köln, Cologne, Germany²
Department of Dermatology, New England Medical Center, Boston, MA, USA³
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA⁴

Author for correspondence: Hans-Ulrich Bernard. Fax +65 779 1117. e-mail mcbhub{at}imcb.nus.edu.sg

The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6–CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.

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