Correction: Corrigendum: Sequences flanking the core-binding site modulate glucocorticoid receptor structure and activity

Abstract The glucocorticoid receptor (GR) binds as a homodimer to genomic response elements, which have particular sequence and shape characteristics. Here we show that the nucleotides directly flanking the core-binding site, differ depending on the strength of GR-dependent activation of nearby genes. Our study indicates that these flanking nucleotides change the three-dimensional structure of the DNA-binding site, the DNA-binding domain of GR and the quaternary structure of the dimeric complex. Functional studies in a defined genomic context show that sequence-induced changes in GR activity cannot be explained by differences in GR occupancy. Rather, mutating the dimerization interface mitigates DNA-induced changes in both activity and structure, arguing for a role of DNA-induced structural changes in modulating GR activity. Together, our study shows that DNA sequence identity of genomic binding sites modulates GR activity downstream of binding, which may play a role in achieving regulatory specificity towards individual target genes.

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Determinants for DNA-binding site recognition by the glucocorticoid receptor.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)73988-x ◽

1992 ◽

Vol 267 (35) ◽

pp. 24941-24947

Author(s):

J Zilliacus ◽

A.P. Wright ◽

U Norinder ◽

J.A. Gustafsson ◽

J Carlstedt-Duke

Keyword(s):

Dna Binding ◽

Glucocorticoid Receptor ◽

Binding Site ◽

Dna Binding Site ◽

Site Recognition

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Glucocorticoid receptor binding site in the mouse alpha-amylase 2 gene mediates response to the hormone.

Molecular Endocrinology ◽

10.1210/mend.7.7.8413315 ◽

1993 ◽

Vol 7 (7) ◽

pp. 907-914

Author(s):

E P Slater ◽

H Hesse ◽

J M Müller ◽

M Beato

Keyword(s):

Glucocorticoid Receptor ◽

Binding Site ◽

Receptor Binding ◽

Alpha Amylase ◽

Receptor Binding Site

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AFFINITY LABELING STEROIDS AS BIOLOGICALLY ACTIVE PROBES OF GLUCOCORTICOID RECEPTOR STRUCTURE AND FUNCTION

Molecular Mechanism of Steroid Hormone Action ◽

10.1515/9783110885026.111 ◽

1985 ◽

pp. 111-140 ◽

Cited By ~ 2

Keyword(s):

Glucocorticoid Receptor ◽

Structure And Function ◽

Biologically Active ◽

Affinity Labeling ◽

Receptor Structure ◽

And Function

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Immunoelectron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies.

Journal of Histochemistry & Cytochemistry ◽

10.1177/38.10.1698203 ◽

1990 ◽

Vol 38 (10) ◽

pp. 1405-1411 ◽

Cited By ~ 117

Author(s):

G A Pringle ◽

C M Dodd

Keyword(s):

Monoclonal Antibodies ◽

Binding Site ◽

Core Protein ◽

Collagen Fibrils ◽

Axial Distance ◽

Protein Core ◽

The Core ◽

Microscopic Localization ◽

Tendon Collagen

Two monoclonal antibodies, 6D6 and 7B1, previously shown to recognize different epitopes on different regions of the protein core of decorin were used to localize the protein core in relation to the positively stained bands in the D period of bovine tendon collagen fibrils. Peroxidase-antiperoxidase staining revealed that the antigen is associated with the surface of all fibrils and suggested that the axial distance between antigens is D-periodic. Immunoferritin labeling with each antibody produced a distribution of ferritin particles that showed that both epitopes of the protein core are localized near the d and e bands in the D period. The data indicate that the decorin protein core binding site(s) on tendon collagen fibrils is/are located near these bands, axially, within the D period.

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