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Journal of Virology, July 2000, p. 5872-5879, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

AMF-1/Gps2 Binds p300 and Enhances Its Interaction with Papillomavirus E2 Proteins

Yu-Cai Peng, David E. Breiding, Francis Sverdrup, James Richard, and Elliot J. Androphy*

Department of Dermatology, New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 18 January 2000/Accepted 4 April 2000

The cellular protein AMF-1 (Gps2) positively modulates gene expression by the papillomavirus E2 protein (D. E. Breiding et al., Mol. Cell. Biol. 17:7208-7219, 1997). We show here that AMF-1 also binds the transcriptional coactivator p300 in vitro and in vivo. E2 interacted weakly with p300. These observations led to a model in which AMF-1 recruits p300 into a complex with E2. Cotransfection of AMF-1 or p300 stimulated levels of E2-dependent transcription, while cotransfection of both AMF-1 and p300 showed an additive effect. The functional significance of p300 recruitment for E2 transactivation was evidenced by repression of E2-activated transcription by adenovirus E1A, which inhibits both coactivator and acetylase activities of p300. Antibodies to AMF-1 or E2 immunoprecipitated histone acetylase activity from cell lysates. Western blotting using antibody against acetyl-lysine failed to detect acetylation of AMF-1 or E2 in complex with p300. These results suggest that AMF-1 facilitates the recruitment of p300 and its histone acetylase activity into complexes with E2 and represents a novel mechanism of transcriptional activation.

* Corresponding author. Mailing address: Department of Dermatology, New England Medical Center, Box 166, 750 Washington St., Boston, MA 02111. Phone: (617) 636-1493. Fax: (617) 636-6190. E-mail: eandroph{at}opal.tufts.edu.

Journal of Virology, July 2000, p. 5872-5879, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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