Structural determinants of a glucocorticoid receptor recognition element

Mol Endocrinol. 1990 Dec;4(12):1866-73. doi: 10.1210/mend-4-12-1866.


Analysis of the relative inducibility of an extensive series of mutant glucocorticoid response elements (GREs) defines features critical to the constitution of an active GRE. Assuming that function as a GRE reflects binding of glucocorticoid receptor, our activity data are consistent with the recognition of the GRE as two hexamer half-sites, each half-site recognized by a single subunit of a receptor dimer, probably in a cooperative fashion. Integrity of both half-sites is necessary for an active element, and spacing of the half-sites is critical. The identity of 1 basepair within the hexamer half-site is unconstrained; the receptor probably makes no base-specific contacts at this position. In contrast, at other positions within the half-site, limited substitutions (if any) can be tolerated. These results along with data from certain insertion mutations suggest that the receptor recognizes each hexamer half-site as two separable subelements. A further implication is that the DNA-binding domain of the glucocorticoid receptor is composed of distinct subdomains, which interact with the subelements of the recognition sequence.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Composition
  • Base Sequence
  • Binding Sites
  • Cell Line
  • Chloramphenicol O-Acetyltransferase / genetics
  • DNA / metabolism*
  • Macromolecular Substances
  • Mammary Tumor Virus, Mouse / genetics
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Plasmids
  • Promoter Regions, Genetic / genetics
  • Protein Conformation
  • Receptors, Glucocorticoid / chemistry
  • Receptors, Glucocorticoid / genetics*


  • Macromolecular Substances
  • Receptors, Glucocorticoid
  • DNA
  • Chloramphenicol O-Acetyltransferase