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Originally published In Press as doi:10.1074/jbc.M008625200 on January 2, 2001

J. Biol. Chem., Vol. 276, Issue 13, 10413-10422, March 30, 2001
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Physical Interaction between the MADS Box of Serum Response Factor and the TEA/ATTS DNA-binding Domain of Transcription Enhancer Factor-1*

Madhu GuptaDagger , Paul Kogut§, Francesca J. Davis§, Narasimhaswamy S. Belaguli, Robert J. Schwartz, and Mahesh P. Gupta§||

From the Dagger  Heart Institute for Children and Department of Physiology and Biophysics, University of Illinois, Chicago, Illinois 60612 § Department of Surgery (Division of Cardiac and Thoracic), University of Chicago, Chicago, Illinois 60637, and  Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030

Serum response factor is a MADS box transcription factor that binds to consensus sequences CC(A/T)6GG found in the promoter region of several serum-inducible and muscle-specific genes. In skeletal myocytes serum response factor (SRF) has been shown to heterodimerize with the myogenic basic helix-loop-helix family of factors, related to MyoD, for control of muscle gene regulation. Here we report that SRF binds to another myogenic factor, TEF-1, that has been implicated in the regulation of a variety of cardiac muscle genes. By using different biochemical assays such as affinity precipitation of protein, GST-pulldown assay, and coimmunoprecipitation of proteins, we show that SRF binds to TEF-1 both in in vitro and in vivo assay conditions. A strong interaction of SRF with TEF-1 was seen even when one protein was denatured and immobilized on nitrocellulose membrane, indicating a direct and stable interaction between SRF and TEF-1, which occurs without a cofactor. This interaction is mediated through the C-terminal subdomain of MADS box of SRF encompassing amino acids 204-244 and the putative 2nd and 3rd alpha -helix/beta -sheet configuration of the TEA/ATTS DNA-binding domain of TEF-1. In the transient transfection assay, a positive cooperative effect of SRF and TEF-1 was observed when DNA-binding sites for both factors, serum response element and M-CAT respectively, were intact; mutation of either site abolished their synergistic effect. Similarly, an SRF mutant, SRFpm-1, defective in DNA binding failed to collaborate with TEF-1 for gene regulation, indicating that the synergistic trans-activation function of SRF and TEF-1 occurs via their binding to cognate DNA-binding sites. Our results demonstrate a novel association between SRF and TEF-1 for cardiac muscle gene regulation and disclose a general mechanism by which these two super families of factors are likely to control diversified biological functions.

* This work was supported by Grant-in-aid 150108N from American Heart Association National Center, University of Chicago Surgery Research Committee grant, Hartford Foundation Center of Excellence grant, Scientist Development Award 9930328Z from American Heart Association-Midwest Affiliate, and National Institutes of Health Grant RO-1 HL-45646.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Surgery (Cardiac and Thoracic), MC 5040, the University of Chicago, Chicago, IL 60637. Tel.: 773-834-4648; Fax: 773-702-4187; E-mail: mgupta@surgery.bsd.uchicago.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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