Reports

Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily

Science  24 Nov 1995:
Vol. 270, Issue 5240, pp. 1354-1357
DOI: 10.1126/science.270.5240.1354

Abstract

A yeast two-hybrid system was used to identify a protein that interacts with and enhances the human progesterone receptor (hPR) transcriptional activity without altering the basal activity of the promoter. Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). Coexpression of SRC-1 reversed the ability of the estrogen receptor to squelch activation by hPR. Also, the amino terminal truncated form of SRC-1 acted as a dominant-negative repressor. Together, these results indicate that SRC-1 encodes a coactivator that is required for full transcriptional activity of the steroid receptor superfamily.

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