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Mechanism Of High-Mobility Group Protein B Enhancement Of Progesterone Receptor Sequence-Specific Dna Binding, James S. Adelman, Sarah C. Roemer, Mair E.A. Churchill, Dean P. Edwards
Mechanism Of High-Mobility Group Protein B Enhancement Of Progesterone Receptor Sequence-Specific Dna Binding, James S. Adelman, Sarah C. Roemer, Mair E.A. Churchill, Dean P. Edwards
James S. Adelman
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 …