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DNA-binding by the glucocorticoid receptor: a structural and functional analysis.

K Dahlman-Wright¹, A Wright, J Carlstedt-Duke

¹Department of Medical Nutrition, Huddinge Hospital, Karolinska Institute, Sweden.

The Journal of Steroid Biochemistry and Molecular Biology

|March 1, 1992

Summary

Researchers studied the glucocorticoid receptor

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Area of Science:

Molecular Biology
Structural Biology
Endocrinology

Background:

The glucocorticoid receptor (GR) is a ligand-activated nuclear receptor crucial for cellular responses.
Nuclear receptors share conserved DNA-binding domains, suggesting common recognition mechanisms.
Understanding GR DNA binding is key to deciphering gene regulation by steroid hormones.

Purpose of the Study:

To characterize the DNA-binding domain (DBD) of the glucocorticoid receptor.
To investigate the structural basis of DNA sequence recognition by GR.
To compare GR DNA-binding mechanisms with other nuclear receptors.

Main Methods:

Expression and purification of the GR DNA-binding domain in E. coli.
Biochemical assays to assess DNA binding affinity and specificity.

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Structural studies, including three-dimensional structure determination.

Main Results:

The purified GR DBD binds to specific DNA sequences, confirming its suitability for structural studies.
GR DBD binds DNA as a dimer, mediated by protein-protein interactions near the C-terminal zinc-binding site.
A specific N-terminal segment dictates target DNA sequence recognition for GR and estrogen receptors.
The GR DBD structure differs from the TFIIIA-type zinc-binding domain, revealing a unique DNA recognition motif.

Conclusions:

The glucocorticoid receptor DNA-binding domain is structurally distinct from TFIIIA-type zinc-binding domains.
Protein-protein interactions and specific sequence elements within the GR DBD are critical for DNA binding and recognition.
This study provides insights into the molecular mechanisms of nuclear receptor-mediated gene regulation.