Nucleic Acids Research, 1994, Vol. 22, No. 15 3053-3060
© 1994
MOLECULAR BIOLOGY |
An adenovirus E1A transcriptional repressor domain functions as an activator when tethered to a promoter
Department of Cell and Molecular Biology, The Medical Nobel InstituteKarolinska Institutet S-171 77 Stockholm, Sweden
*To whom correspondence should be addressed
Received May 6, 1994. Revised July 5, 1994. Accepted July 5, 1994.
The adenovirus E1A protein contains three well conserved regions, designated conserved region (CR) 1, 2 and 3, which are important for the multiple activities ascribed to E1 A. The CR3 domain constitutes a prototypic transcription activator, consisting of a promoter targeting region and a transactivating region. Here we demonstrate the existence of a second transactivating region located within amino acids 28 to 90 (essentially the CR1 domain) of the E1A protein. A fusion protein, containing the Gal4 DNA binding domain linked to CR1, was as efficient as the classical CR3 transactivator in activating transcription from a reporter plasmid containing Gal4 binding sites. However, competition experiments suggest that Gal/CR1 and Gal/CR3 work through different cellular targets. The E1A-243R protein has previously been extensively characterized as a repressor of transcription. Here we show that a Gal4 fusion protein expressing the CR1 domain is indeed sufficient for repression of SV40 enhancer activity. Collectively, our results suggest that CR1 functions as an activator if tethered to a promoter and as a repressor in the absence of promoter association.
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