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J Biol Chem, Vol. 275, Issue 10, 7313-7320, March 10, 2000

The N-terminal Region of the Human Progesterone A-receptor
STRUCTURAL ANALYSIS AND THE INFLUENCE OF THE DNA BINDING DOMAIN*

David L. BainDagger §, Mary A. FrandenDagger , James L. McManaman, Glenn S. TakimotoDagger , and Kathryn B. HorwitzDagger

From the Dagger  Department of Medicine and Molecular Biology Program and the  Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262

The role of the N-terminal region in nuclear receptor function was addressed by a biochemical and biophysical analysis of the progesterone receptor A-isoform lacking only the hormone binding domain (NT-A). Sedimentation studies demonstrate that NT-A is quantitatively monomeric, with a highly asymmetric shape. Contrary to dogma, the N-terminal region is structured as demonstrated by limited proteolysis. However, N-terminal structure is strongly stabilized by the DNA binding domain, possibly explaining the lack of structure seen in isolated activation domains. Upon DNA binding, NT-A undergoes N-terminal mediated assembly, suggestive of DNA-induced allostery, and consistent with changes in protease accessibility of sites outside the DNA binding domain. Microsequencing reveals that protease-accessible regions are limited to previously identified phosphorylation motifs and to functional domain boundaries.

* This work was supported by a grant from the Cancer League of Colorado (to D. L. B.), by Grants DK48238 and CA26869 from the National Institutes of Health (to K. B. H.), and by the DNA Sequencing, Protein Chemistry and Tissue Culture core laboratories of the Cancer Center of the University of Colorado Health Sciences Center.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 correspondence should be addressed: Dept. of Medicine, 4200 E. Ninth Ave., B-151, University of Colorado Health Sciences Center, Denver, CO 80262. Tel.: 303-315-8850; Fax: 303-315-4525; E-mail: david.bain@uchsc.edu.

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