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Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding
Nucleic Acids Research (2008)
  • James S. Adelman
  • Sarah C. Roemer
  • Mair E.A. Churchill
  • Dean P. Edwards, Baylor College of Medicine
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.
  • HMGB,
  • Proteins,
  • Peptides,
  • Receptors,
  • Progesterone,
  • DNA,
  • Adenine,
  • Thymine
Publication Date
Publisher Statement
This article is from Nucleic Acids Research 36 (2008): 3655, doi:10.1093/nar/gkn249. Posted with permission.
Citation Information
James S. Adelman, Sarah C. Roemer, Mair E.A. Churchill and Dean P. Edwards. "Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding" Nucleic Acids Research Vol. 36 Iss. 11 (2008)
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