Glucocorticoid receptor binds half sites as a monomer and regulates specific target genes.

ABSTRACT:

Background

Glucocorticoid receptor (GR) is a hormone-activated, DNA-binding transcriptional regulatory factor that controls inflammation, metabolism, stress responses, and other physiological processes. In vitro, GR binds as an inverted dimer to a motif consisting of two imperfectly palindromic 6 bp half sites separated by 3 bp spacers. In vivo, GR employs different patterns of functional surfaces of GR to regulate different target genes. The relationships between GR genomic binding and functional surface utilization have not been defined.

Results

We find that A477T, a GR mutant that disrupts the dimerization interface, differs from wild-type GRα in binding and regulation of target genes. Genomic regions strongly occupied by A477T are enriched for a novel half site motif. In

SUBMITTER: Schiller BJ 

PROVIDER: S-EPMC4149261 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature