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Nucleic Acids Research Advance Access published online on May 12, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn249
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding

Sarah C. Roemer1, James Adelman1, Mair E. A. Churchill1,2 and Dean P. Edwards3,*

1Program in Molecular Biology, 2Department of Pharmacology, University of Colorado Denver, School of Medicine, Aurora, CO 80045 and 3Department of Molecular and Cellular Biology and Pathology, Baylor College of Medicine, Houston, TX 77030, USA

*To whom correspondence should be addressed. Tel: +1 713 798 2326; Fax: +1 713 798 2717; Email: deane{at}bcm.edu

Received January 18, 2008. Revised April 18, 2008. Accepted April 20, 2008.

The DNA-binding domain (DBD) of progesterone receptor (PR) is bipartite containing a zinc module core that interacts with progesterone response elements (PRE), and a short flexible carboxyl terminal extension (CTE) that interacts with the minor groove flanking the PRE. The chromosomal high-mobility group B proteins (HMGB), defined as DNA architectural proteins capable of bending DNA, also function as auxiliary factors that increase the DNA-binding affinity of PR and other steroid receptors by mechanisms that are not well defined. Here we show that the CTE of PR contains a specific binding site for HMGB that is required for stimulation of PR-PRE binding, whereas the DNA architectural properties of HMGB are dispensable. Specific PRE DNA inhibited HMGB binding to the CTE, indicating that DNA and HMGB–CTE interactions are mutually exclusive. Exogenous CTE peptide increased PR-binding affinity for PRE as did deletion of the CTE. In a PR-binding site selection assay, A/T sequences flanking the PRE were enriched by HMGB, indicating that PR DNA-binding specificity is also altered by HMGB. We conclude that a transient HMGB–CTE interaction alters a repressive conformation of the flexible CTE enabling it to bind to preferred sequences flanking the PRE.


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