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Originally published In Press as doi:10.1074/jbc.M008274200 on November 22, 2000

J. Biol. Chem., Vol. 276, Issue 5, 2992-2997, February 2, 2001
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Cooperative Mechanism of Transcriptional Activation by a Cyclic AMP-response Element Modulator alpha  Mutant Containing a Motif for Constitutive Binding to CREB-binding Protein*

Daniel M. FassDagger , Johanna C. CraigDagger , Soren Impey, and Richard H. Goodman§

From the Vollum Institute, Oregon Health Sciences University, Portland, Oregon 97201

Cyclic AMP-response element modulator alpha  (CREMalpha ) is a transcription factor that is highly related to cAMP-response element-binding protein (CREB) but represses cAMP-induced gene expression from simple artificial promoters containing a cAMP-response element (CRE). CREMalpha lacks two glutamine-rich Q regions that, in CREB, are thought to be necessary for transcriptional activation. Nevertheless, protein kinase A stimulation induces CREMalpha to activate the complex native promoter in the phosphoenolpyruvate carboxykinase (PEPCK) gene. To study this phenomenon in the absence of protein kinase A stimulation, we introduced a mutation into CREMalpha to allow constitutive binding to the coactivator CREB-binding protein. This mutant, CREMalpha DIEDML, constitutively activated the PEPCK promoter. By engineering the leucine zipper regions of CREMalpha DIEDML and CREBDIEDML to direct their patterns of dimerization, we found that only CREMalpha DIEDML homodimers fully activated the PEPCK promoter. By using a series of deletion and block mutants of the PEPCK promoter, we found that activation by CREMalpha DIEDML depended on the CRE and two CCAAT/enhancer-binding protein (C/EBP) sites. A dominant negative inhibitor of C/EBP, A-C/EBP, suppressed activation by CREMalpha DIEDML. Furthermore, a GAL4-C/EBPalpha fusion protein and CREMalpha DIEDML cooperatively activated a promoter containing three GAL4 sites and the PEPCK CRE. Thus, we propose that the C/EBP sites in the PEPCK promoter allow CREMalpha to activate transcription despite its lack of Q regions.

* This work was supported by grants 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 These authors contributed equally to this work.

§ To whom correspondence should be addressed: Vollum Inst., Oregon Health Sciences University, 3181 S. W. Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-494-5078; Fax: 503-494-4353; E-mail: goodmanr@ohsu.edu.

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