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A more recent version of this article appeared on October 27, 2000
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Papers In Press, published online ahead of print August 2, 2000
J. Biol. Chem, 10.1074/jbc.M003043200
Submitted on April 11, 2000
Revised on July 13, 2000
Accepted on August 2, 2000

Role for p300 in PAX 8 induction of tyroperoxidase gene expression

Rossana De Leo, Stefania Miccadei, Enrico Zammarchi, and Donato Civitareale

Molecular Pathology Laboratory, Regina Elena Cancaer Institute, Rome, Italy 00158

Corresponding Author: dciv{at}yahoo.com

The nuclear p300 protein functions as co-activator of gene transcription. Here, we show that p300 works as co-activator of the transcription factor Pax 8 on Thyroperoxidase gene promoter. Consistent with its role as co-activator, p300 potentiates Pax 8 activated transcription. Furthermore we provide evidences supporting the formation of a complex between both factors in vivo and in vitro. This interaction involves the N-terminal domain and the CH3 domain of p300 and the trans-activation domain of Pax 8 at its C-terminal end. We show that the CH3 domain is crucial for the co-activator role of p300 on Thyroperoxidase gene promoter. In agreement with our finding and with the ability of the adenoviral protein E1A to bind p300, we show that E1A down-regulates Pax 8 activity.


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