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Originally published In Press as doi:10.1074/jbc.M007824200 on November 16, 2000

J. Biol. Chem., Vol. 276, Issue 7, 5213-5221, February 16, 2001
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Induction-independent Recruitment of CREB-binding Protein to the c-fos Serum Response Element through Interactions between the Bromodomain and Elk-1*

L. Johan NissenDagger , Jean-Christophe Gelly, and Robert A. Hipskind§

From the Institut de Génétique Moléculaire de Montpellier, IFR24, CNRS, 1919 Rte. de Mende, Montpellier 34293, France

Proliferative signals lead to the rapid and transient induction of the c-fos proto-oncogene by targeting the ternary complex assembled on the serum response element (SRE). Transactivation by both components of this complex, serum response factor (SRF) and the ternary complex factor Elk-1, can be potentiated by the coactivator CREB-binding protein (CBP). We report a novel interaction between the bromodomain of CBP, amino acids 1100-1286, and Elk-1. DNA binding and glutathione S-transferase pull-down assays demonstrate that binding requires Elk-11-212 but not the C-terminal transactivation domain. Competition and antibody controls show that the bromocomplex involves both SRF and Elk-1 on the c-fos SRE and uniquely Elk-1 on the E74 Ets binding site. Interestingly, methylation interference and DNA footprinting analyses show almost indistinguishable patterns between ternary and bromocomplexes, suggesting that CBP-(1100-1286) interacts via Elk-1 and does not require specific DNA contacts. Functionally, the bromocomplex blocks activation, because cotransfection of CBP-(1100-1286) reduces RasV12-driven activation of SRE and E74 luciferase reporters. Repression is relieved moderately or strongly by linking the bromodomain to the N- or C-terminal transactivation domains of CBP, respectively. These results are consistent with a model in which CBP is constitutively bound to the SRE in a higher order complex that would facilitate the rapid transcriptional activation of c-fos by signaling-driven phosphorylation.

* This work was supported in part by grants from the French Association pour la Recherche sur le Cancer and Fondation pour la Recherche Medicale, as well as from the Pharma Division of Novartis, S.A.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 Received support for some research costs from The Danish Research Academy.

§ To whom correspondence should be addressed: Tel.: 33-467-613-667; Fax: 33-467-040-231; E-mail: hipskind@jones.igm.cnrs-mop.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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