Polyomavirus large T antigen binds the transcriptional coactivator protein p300.
Using coimmunoprecipitation and glutathione S-transferase pulldown experiments, we found that polyomavirus large T antigen binds to p300 in vivo and in vitro. The N-terminal region of the viral protein, including the pRB binding motif, was dispensable for this interaction, which involved several regions within the C-terminal half of the large T antigen. Interestingly, anti-T antibody coimmunoprecipitated a subspecies of p300 which has high histone acetyltransferase activity.
Nemethova
M
M
Institut für Molekularbiologie der Universität Wien, Wiener Biozentrum, A-1030 Vienna, Austria.
Wintersberger
E
E
D016475:3T3 Cells; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism; D002461:Cell Line, Transformed; D050881:E1A-Associated p300 Protein; D051548:Histone Acetyltransferases; D051379:Mice; D009687:Nuclear Proteins / Q000378:metabolism*; D015534:Trans-Activators / Q000378:metabolism*; D014157:Transcription Factors; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor
D000123:Acetyltransferases; D000952:Antigens, Polyomavirus Transforming; D018797:Cell Cycle Proteins; D050881:E1A-Associated p300 Protein; D051548:Histone Acetyltransferases; D009687:Nuclear Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor; C494361:Ep300 protein, mouse