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Originally published In Press as doi:10.1074/jbc.M207466200 on January 16, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10578-10587, March 21, 2003
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Conformation of CCAAT/Enhancer-binding Protein alpha  Dimers Varies with Intranuclear Location in Living Cells*

Fred SchaufeleDagger §, Xia WangDagger , Xiaowei LiuDagger , and Richard N. Day

From the Dagger  Diabetes Center, Metabolic Research Unit and Department of Medicine, University of California, San Francisco, California 94143-0540 and  Departments of Medicine and Cell Biology, National Science Foundation Center for Biological Timing, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908

The structure of a protein defines its biochemical properties, but the impact of intracellular location and environment on protein structure remains poorly defined. CCAAT/enhancer-binding protein alpha  (C/EBPalpha ) is a master regulator of transcription and cellular proliferation that concentrates and is kept inactive at transcriptionally quiescent, pericentromeric regions in mouse cell nuclei. C/EBPalpha dimer structure was measured in living cells from the amounts of fluorescence energy transferred between derivatives of the green fluorescent protein attached to different C/EBPalpha domains. Comparing the levels of fluorescence resonance energy transfer at pericentromeric and nonpericentromeric regions of the nucleus indicated that the DNA binding domains of C/EBPalpha dimers were further apart and interacted more poorly at pericentromeric heterochromatin than in the more euchromatic regions of the nucleus. In contrast, the position and interactions of the transcriptional activation domains were similar throughout the nucleus. Phorbol ester treatment caused a shift in the position of the transcriptional activation domain relative to the DNA binding domain. Thus, C/EBPalpha conformation varies with intranuclear location and with cellular environment. These "fluorescence resonance energy transfer nanoscopy" techniques will be broadly applicable for associating conformational and kinetic variations to subcompartment-specific actions of C/EBPalpha or any protein in the dynamic intracellular environment.

* This work was supported by National Institutes of Health Grant DK 54345 and grants from the University of California San Francisco Research Evaluation and Allocation Committee and from the University of California San Francisco Committee on Research (to F. S.).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.

§ To whom all correspondence should be addressed. Tel.: 415-476-7086; Fax: 415-564-5813; E-mail: freds@diabetes.ucsf.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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