Open AccessAMF-1/Gps2 Binds p300 and Enhances Its Interaction with Papillomavirus E2 Proteins
Author(s) -
Yu Cai Peng,
David E. Breiding,
Francis M. Sverdrup,
J Gibbons Richard,
Elliot J. Androphy
Publication year - 2000
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.74.13.5872-5879.2000
Subject(s) - transactivation , coactivator , biology , microbiology and biotechnology , histone , p300 cbp transcription factors , histone acetyltransferase , transcription (linguistics) , bovine papillomavirus , transcription factor , acetylation , immunoprecipitation , gene , genetics , histone acetyltransferases , linguistics , philosophy , genome
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.