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Papers In Press, published online ahead of print January 2, 2001
Surgery (Cardiac & thoracic), MC 5040, University of Chicago, Chicago, IL 60637
Corresponding Author: mgupta{at}surgery.bsd.uchicago.edu
ABSTRACT Serum responce factor is a MADS box transcription factor which binds to consensus sequences CC(A/T)6GG found in the promoter region of several serum-inducible and muscle-specific genes. In skeletal myocytes SRF has been shown to hetrodimerize 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-pull down assay and co-immunoprecipitation of proteins we showed 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 c-terminal subdomian of MADS box of SRF encompasing 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, SRE and M-CAT respectively, were intact; mutation of either site abolished their synergistic effect. Similarly a SRF mutant, SRFpm-1, defective in DNA binding failed to collaborate with TEF-1 for gene regulation, indicating that the synergistic transactivation 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 superfamilies of factors are likely to control diversified biological functions.
J. Biol. Chem, 10.1074/jbc.M008625200
Submitted on September 20, 2000
Revised on January 2, 2001
Accepted on December 29, 2000
Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1
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