Molecular and Cellular Biology, April 1999, p. 2577-2584, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
-Actin Promoter

Institute for Genetic Medicine and Department of Biochemistry and Molecular Biology, University of Southern California School of Medicine, Los Angeles, California,1 and Institute of Chemistry, University of Brescia School of Medicine, Brescia, Italy2
Received 17 September 1998/Returned for modification 3 December 1998/Accepted 4 January 1999
Activation of the human cardiac
-actin (HCA) promoter in
skeletal muscle cells requires the integrity of DNA binding sites for
the serum response factor (SRF), Sp1, and the myogenic basic helix-loop-helix (bHLH) family. In this study we report that activation of the HCA correlates with formation of a muscle-specific
multiprotein complex on the promoter. We provide evidence that
proteins eluted from the multiprotein complex specifically react with
antibodies directed against myogenin, Sp1, and SRF and that the complex
can be assembled in vitro by using the HCA promoter and purified
MyoD, E12, SRF, and Sp1. In vitro and in vivo assays revealed a direct association of Sp1 and myogenin-MyoD mediated by the DNA-binding domain
of Sp1 and the HLH motif of myogenin. The results obtained in this
study indicate that protein-protein interactions and the cooperative
DNA binding of transcriptional activators are critical steps in the
formation of a transcriptionally productive multiprotein complex on the
HCA promoter and suggest that the same mechanisms might be
utilized to regulate the transcription of muscle-specific and other genes.
Present address: Molecular Neurobiology, Children's Hospital of
Orange County, Orange, Calif.
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