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Nucleic Acids Research, 1995, Vol. 23, No. 6 925-931
© 1995
MOLECULAR BIOLOGY |
Functional interactions between YY1 and adenovirus E1A
1Department of Pathology, Harvard Medical School 200 Longwood Avenue, Boston, MA 02115, USA 2Committee on Virology, Harvard Medical School 200 Longwood Avenue, Boston, MA 02115, USA 3Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute Boston, MA 02115, USA
*To whom correspondence should be addressed
Received December 14, 1994. Revised January 27, 1995. Accepted January 27, 1995.
YY1 is a C2H2-type zinc finger transcription factor that is a member of the human GLI-Kruppel family of proteins. YY1 represses transcription when bound upstream of transcription initiation sites. The repression can be relieved by adenovirus E1A and activation of target genes occurs. We have mapped the repression domain of YY1 to the C-terminal region, overlapping Its DNA binding domain. We have also identified an activation domain within the first 69 amino acids of YY1. The YY1 C-terminal region is involved in physical Interactions with E1A and is functionally necessary for YY1to respond to E1 A. This suggests that relief of YY1 repression by E1A involves YY1-E1A physical interactions. Although not involved in Interactions with E1A, the N-terminal activation domain is also necessary for YY1 to respond to E1A. Presumably, under repressing conditions, the activation domain Is masked by the conformation of YY1, but is released upon bindingof E1A and is required to subsequently activate transcription. Consistent with this hypothesis, an ATF-2-YY1 chimeric protein containing the activation domain of ATF-2 and the C-terminal two-thirds of YY1 is still a potent repressor. Unlike themutant YY1 lacking its own N-terminal activation domain, the chimeric protein is fully responsive to E1A.
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