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Nucleic Acids Research, Vol 27, Issue 3 866-874, Copyright © 1999 by Oxford University Press

ARTICLES

PolyADP-ribose polymerase is a coactivator for AP-2-mediated transcriptional activation

P Kannan, Y Yu, S Wankhade and MA Tainsky
Rammelkamp Center for Education and Research, MetroHealth Campus, Case Western Reserve University,2500 MetroHealth Drive, Cleveland, OH 44109, USA. pkannan@research.mhmc.org

Overexpression of transcription factor AP-2 has been implicated in the tumorigenicity of the human teratocarcinoma cell lines PA-1 that contain an activated ras oncogene. Here we show evidence that overexpression of AP-2 sequesters transcriptional coactivators which results in self-inhibition. We identified AP-2-interacting proteins and determined whether these proteins were coactivators for AP-2-mediated transcription. One such interacting protein is polyADP-ribose polymerase (PARP). PARP suppresses AP-2 self-inhibition and enhances AP- 2 activity in PA-1 cells indicating that it is a coactivator for AP-2- transcription. PARP significantly restores AP-2 transcriptional activity in ras oncogene-transformed cells suggesting that it might suppress transformation in these cells. Another AP-2-interacting protein, RAP74, a subunit of transcription factor TFIIF, does not affect AP-2-mediated transcriptional activation alone or in the presence of RAP30, the other subunit of TFIIF. RAP74 also fails to relieve AP-2-mediated transcriptional self-interference and cross- interference. These studies suggest that the interaction between AP-2 and RAP74 may have functions other than activation of AP-2-mediated transcription.
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