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A more recent version of this article appeared on August 31, 2001
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M104963200v1
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Papers In Press, published online ahead of print July 3, 2001
J. Biol. Chem, 10.1074/jbc.M104963200
Submitted on May 30, 2001
Revised on July 2, 2001
Accepted on July 2, 2001

The DNA glycosylase TDG represses TTF-1 activated transcription by direct association

Caterina Missero, Maria Teresa Pirro, Silvana Simeone, Michele Pischetola, and Roberto Di Lauro

Telethon Institute for Genetics and Medicine, Napoli 80131

Corresponding Author: missero{at}tigem.it

The transcription factor TTF-1 is a homeodomain-containing protein that belongs to the NK2 family of genes involved in organogenesis. TTF-1 is required for normal development of the forebrain, lung and thyroid. In a search for factors that regulate TTF-1 transcriptional activity, we isolated three genes (TDG, HIPK2 and Ajuba), whose products can interact with TTF-1 in yeast and in mammalian cells. TDG (T:G mismatch thymine glycosylase) is an enzyme involved in base excision repair. In the present manuscript we show that TDG acts as a strong repressor of TTF-1 transcriptional activity in a dose-dependent manner, while HIPK2 and Ajuba display no effect on TTF-1 activity at least under the tested conditions. TDG-mediated inhibition occurs specifically on TTF-1 responsive promoters in thyroid and non thyroid cells. TDG associates with TTF-1 in mammalian cells through the TTF-1 carboxy-terminal activation domain and is independent of the homeodomain. These findings reveal a previously unsuspected role for the repair enzyme TDG as a transcriptional repressor, and open new routes toward the understanding of the regulation of TTF-1 transcriptional activity.


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