Abstract
Interferon-"/ (IFN-7) induces rapid tyrosine phosphorylation of the latent cytoplasmic transcription factor. Statl, which then forms homodimers, translocates to the nucleus and participates in IFN-7-induced transcription. However, little is known of the interactions between Statl and the general transcription machinery during transcriptional activation. We show here that Statl can directly interact with the CBP/p300 family of transcriptional coactivators. Specifically, two interaction regions were identified: the amino terminal region of Statl interacts with the CREB-binding domain of CBP/p300 and the carboxyl terminal region of Statl interacts with the domain of CBP/p300 that binds adenovirus E1A protein. Transfection experiments suggest a role for these interactions in IFN-7-induced transcription. Because CBP/p300-binding is required for the adenovirus E1A protein to regulate transcription of many genes during viral replication and cellular transformation, it is possible that the anti-viral effect of IFN-7 is based at least in part on direct competition by nuclear Statl with E1A for CBP/p300 binding.
Original language | English (US) |
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Pages (from-to) | A1072 |
Journal | FASEB Journal |
Volume | 11 |
Issue number | 9 |
State | Published - Dec 1 1997 |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Genetics