Polyomavirus Large T Antigen Binds the Transcriptional Coactivator Protein p300

AUTOR(ES)

Nemethova, Maria

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Corrigendum: The SV40 large T antigen and adenovirus E1a oncoproteins interact with distinct isoforms of the transcriptional co-activator, p300
• Regulation of β-catenin transformation by the p300 transcriptional coactivator
• HIV transcriptional activation by the accessory protein, VPR, is mediated by the p300 co-activator
• p300 Acts as a Transcriptional Coactivator for Mammalian Notch-1
• Association of p300 and CBP with simian virus 40 large T antigen.