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J. Biol. Chem., Vol. 279, Issue 53, 55017-55023, December 31, 2004

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The N Termini of Friend of GATA (FOG) Proteins Define a Novel Transcriptional Repression Motif and a Superfamily of Transcriptional Repressors^*

Andy C. Lin, Andrea E. Roche¶, Jeannine Wilk¶, and Eric C. Svensson¶||

From the Department of Medicine, Stanford University, Stanford, California 94305 and ^¶Department of Medicine, University of Chicago, Chicago, Illinois 60637

Members of the Friend of GATA (FOG) family of transcriptional co-factors are required for the development of both the cardiovascular and hematopoietic systems. FOG proteins physically interact with members of the GATA family of transcriptional activators and modulate their activity. We have previously shown that FOG-2 can bind to the N-terminal zinc finger of GATA4 and, via this interaction, repress GATA4-mediated transcriptional activation of various cardiac promoters. In this report we further characterize the domain of FOG-2 necessary for repression of GATA4 transcriptional activity. We show that FOG-2-mediated repression is not blocked by the histone deacetylase inhibitor tricostatin A, suggesting that FOG-2 repression of GATA4 occurs via a histone deacetylase independent mechanism. N-terminal deletion mutants of FOG-2 revealed that the first 12 amino acids of FOG-2 are necessary for FOG-2-mediated repression. Fusion of these 12 amino acids to the DNA binding domain of GAL4 demonstrated that this region is sufficient to mediate transcriptional repression even when recruited to a heterologous promoter. Single amino acid substitutions within this N-terminal domain of FOG-2 defined the critical amino acid sequence as RRKQxxPxxI. Interestingly, a search of the NCBI protein data base identified several other partially characterized zinc finger transcriptional repressors from various vertebrate species that contained this motif at their N terminus. Taken together, these observations define a novel transcriptional repression motif and a superfamily of zinc finger transcriptional repressors.

Received for publication, October 1, 2004 , and in revised form, October 21, 2004.

^* This work was supported by National Institutes of Health Grant HL071063, the American Heart Association, and the Schweppe Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

^|| To whom correspondence should be addressed: Section of Cardiology, Dept. of Medicine, University of Chicago, 5841 S. Maryland Ave, MC6088, Chicago, IL 60637. Tel.: 773-834-0313; Fax: 773-702-2681; E-mail: esvensso{at}medicine.bsd.uchicago.edu.

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