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A more recent version of this article appeared on March 29, 2002
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Papers In Press, published online ahead of print January 23, 2002
J. Biol. Chem, 10.1074/jbc.M110228200
Submitted on October 24, 2001
Revised on December 31, 2001
Accepted on January 23, 2002

Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via HLH domain, MEF2 interaction and chromatin deacetylation

Xue Q. Gong and Li Li

Internal Medicine, Center for Molecular Medicine and Genetics, Wayne State University, Detroit, MI 48201

Corresponding Author: lili{at}med.wayne.edu

Dermo-1 is a multifunctional bHLH transcription factor that has been shown to be a potent negative regulator for gene transcription and apoptosis. To understand the molecular mechanisms that mediate the function of Dermo-1, we generated a series of Dermo-1 mutants and used a MyoD-mediated transcriptional activation model to characterize the roles of its N-terminal, bHLH, and C-terminal structural domains in transcriptional repression. Both the C-terminal and HLH domains of Dermo-1 were essential for its repression of MyoD-mediated transactivation. Dermo-1 repressed, in a dose-dependent fashion, the transactivation activity of MEF2, a protein known to cooperate with MyoD in activating E-box-dependent gene expression. Both the N- and C-terminal domains of Dermo-1, but not the bHLH domain, were required for the inhibition of MEF2, suggesting that Dermo-1 inhibits both MyoD- and MEF2-dependent transactivation but through different mechanisms. Dermo-1 interacted directly with MEF2 and selectively repressed the MEF2 transactivation domain. An overall increase of histone acetylation induced by trichostatin A (TSA) treatment reduced Dermo-1 transcriptional repression activity, suggesting that histone deacetylation is involved in Dermo-1-mediated transcriptional repression. Together, these results suggest that MEF2 is an important target in Dermo-1-mediated transcriptional repression and provide initial evidence of the involvement of histone acetylation in Dermo-1 transcriptional repression.


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