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Originally published In Press as doi:10.1074/jbc.M909810199 on March 15, 2000
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J Biol Chem, Vol. 275, Issue 20, 15557-15562, May 19, 2000

The Bradykinin Type 2 Receptor Is a Target for p53-mediated Transcriptional Activation*

Zubaida Saifudeen, Hong Du, Susana Dipp, and Samir S. El-DahrDagger

From the Department of Pediatrics, Section of Pediatric Nephrology, Tulane University School of Medicine, New Orleans, Louisiana 70112

The bradykinin type 2 receptor (BK2) is a developmentally regulated G protein-coupled receptor that mediates diverse actions such as vascular reactivity, salt and water excretion, inflammatory responses, and cell growth. However, little is known regarding regulation of the BK2 gene. We report here that the rat BK2 receptor is transcriptionally regulated by the tumor suppressor protein p53. The 5'-flanking region of the rat BK2 gene contains two p53-like binding sites: a sequence at -70 base pairs (P1 site) that is conserved in the murine and human BK2 genes; and a sequence at -707 (P2) that is not. The P1 and P2 motifs bind specifically to p53, as assessed by gel mobility shift assays. Transient transfection into HeLa cells of a CAT reporter construct driven by 1.2-kilobases of the BK2 gene 5'-flanking region demonstrated that the BK2 promoter is dose dependently activated by co-expression of wild-type p53. Co-expression of a dominant negative mutant p53 suppresses the activation of BK2 by wild-type p53. Promoter truncation localized the p53-responsive element to the region between -38 and -94 base pairs encompassing the p53-binding P1 sequence. Furthermore, p53-mediated activation of the BK2 promoter is augmented by the transcriptional co-activators, CBP/p300. Interestingly, removal of the P2 site by truncation or site-directed deletion amplifies p53-mediated activation of the BK2 promoter. These results demonstrate that the rat BK2 promoter is a target for p53-mediated activation and suggest a new physiological role for p53 in the regulation of G protein-coupled receptor gene expression.

* This work was supported by Grants DK-53595 and DK-56264 from the National Institutes of Health.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.

Dagger To whom correspondence and reprint requests should be addressed: Tulane University School of Medicine, 1430 Tulane Ave., New Orleans, LA 70112. Tel.: 504-588-5377; Fax: 504-584-1852; E-mail: seldahr@tmcpop.tmc.tulane.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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