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J Biol Chem, Vol. 273, Issue 18, 10831-10834, May 1, 1998

COMMUNICATION
Steroid Receptor Coactivator-1 Interacts with the p50 Subunit and Coactivates Nuclear Factor B-mediated Transactivations

Soon-Young Na, Soo-Kyung Lee^§, Su-Ji Han^¶, Hueng-Sik Choi^¶, Suhn-Young Im^¶, and Jae Woon Lee^§¶

From the  Department of Biology, the ^§ College of Pharmacy, the ^¶ Hormone Research Center, and the  Department of Microbiology, Chonnam National University, Kwangju 500-757, Korea

Steroid receptor coactivator-1 (SRC-1) specifically bound to the transcription factor NFB subunit p50 but not to p65 as demonstrated by the yeast two hybrid tests and glutathione S-transferase pull down assays. The p50-binding site was localized to a subregion of SRC-1 (amino acids 759-1141) that encompasses the previously described CBP-p300-binding domain. In mammalian cells, SRC-1 potentiated the NFB-mediated transactivations in a dose-dependent manner. Coexpression of p300 further enhanced this SRC-1-potentiated level of transactivations, consistent with the recent findings in which CBP and p300 were shown to be transcription coactivators of the p65 subunit (Perkins, N. D., Felzien, L. K., Betts, J. C., Leung, K., Beach, D. H., and Nabel, G. J. (1997) Science 275, 523-527; Gerritsen, M. E., Williams, A. J., Neish, A. S., Moore, S., Shi, Y., and Collins, T. (1997) Proc. Acad. Natl. Sci. U. S. A. 94, 2927-2932). These results suggest that at least two distinct coactivator molecules may cooperate to regulate the NFB-dependent transactivations in vivo and SRC-1, originally identified as a coactivator for the nuclear receptors, may constitute a more widely used coactivation complex.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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