Specificity of Nucleic Acid Structure for Binding Steroid Receptors

Kumar, Salil; Dickerman, Herbert W.

doi:10.1016/b978-0-12-452810-9.50013-9

Cited by 3 publications

(1 citation statement)

References 130 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The rates of activation of covalent and noncovalent complexes seen here were considerably faster than those observed elsewhere (Higgins et al, 1973;Milgrom, 1981;Schmidt & Litwack, 1982;Norris & Kohler, 1983; Kumar & Dickerman, 1983;Vedeckis, 1983a). Several experimental differences could account for the present behavior.…”

Section: Discussioncontrasting

confidence: 43%

Comparison of DNA binding properties of activated, covalent and noncovalent glucocorticoid receptor-steroid complexes from HTC cells

Simons¹,

Miller²

1984

Biochemistry

View full text Add to dashboard Cite

Several differences in the interaction with DNA of noncovalent vs. covalent glucocorticoid receptor-steroid complexes are described. HTC cell glucocorticoid receptors were incubated under cell-free conditions with the potent reversible glucocorticoid dexamethasone and with the irreversible antiglucocorticoid dexamethasone 21-mesylate to yield noncovalent and covalent complexes, respectively. Using DNA immobilized on cellulose, we found that the noncovalent dexamethasone complexes were activated (by dilution in pH 8.8 buffer at 0 degree C) to a DNA binding species 2-fold faster than were covalent dexamethasone 21-mesylate labeled complexes. The affinity of activated, noncovalent dexamethasone complexes for DNA in an equilibrium binding assay was 2-fold higher than that of the activated, covalent dexamethasone 21-mesylate complexes. This conclusion was supported by the observations in a DNA-cellulose pellet assay that covalent receptor-steroid complex binding to DNA was disrupted by lower NaCl concentrations than was noncovalent complex binding. The same studies of DNA binding at various NaCl concentrations failed to provide evidence that glucocorticoid receptor-steroid complex binding to DNA is a multistep process. These quantitative distinctions in the DNA binding properties of covalent and noncovalent receptor-steroid complexes represent the first physicochemical differences between the complexes of antiglucocorticoid and glucocorticoid steroids and may partially account for their divergent biological properties.

show abstract

Section: Discussioncontrasting

confidence: 43%

Comparison of DNA binding properties of activated, covalent and noncovalent glucocorticoid receptor-steroid complexes from HTC cells

Simons¹,

Miller²

1984

Biochemistry

View full text Add to dashboard Cite

show abstract

Inhibition of estrous behavior in rats by intrahypothalamic application of agents that disrupt nuclear binding of estrogen-receptor complexes

Etgen

1987

Hormones and Behavior

View full text Add to dashboard Cite

Identification of a nucleic acid-regulated cyclic gmp-binding activity in Dictyostelium discoideum

Parissenti

Coukell

1989

Journal of Cell Science

View full text Add to dashboard Cite

Using ion-exchange chromatography, we have identified and isolated two forms of a cyclic GMP-specific binding activity in filter-broken cell extracts of Dictyostelium discoideum. Upon addition of excess cold ligand, one form (S-type) released bound 3H-labelled cyclic GMP very slowly (t½ ≈ 68 min), while the other form (F-type) released the cyclic GMP in <1 min. After photoaffinity labelling with 32P-labelled cyclic GMP, both forms revealed a major 160x103Mr band (and a few bands of lower molecular weight) on autoradiograms of sodium dodecyl sulphate-polyacrylamide gels. Addition of 500 mM-NaCl to S-type activity converted the activity to a fast-dissociating form indistinguishable from F-type, and this conversion was reversed by dialysis. Salt treatment or dialysis had no appreciable effect on the association/dissociation kinetics of F-type activity. When crude S-type activity was heated (to destroy cyclic GMP binding) and then added to F-type activity, the latter activity acquired slow-dissociating properties identical to S-type. This result suggested that the cells possess a ‘factor’ that can dramatically alter binding properties of this cyclic GMP-binding protein. Crude preparations of this factor were by boiling or proteases, but were sensitive to RNase A. Further studies revealed that acids (in particular, DNA) could effectively mimic the factor in its ability to modulate the binding kinetics of the cyclic GMP-binding activity.

show abstract

Specificity of Nucleic Acid Structure for Binding Steroid Receptors

Cited by 3 publications

References 130 publications

Comparison of DNA binding properties of activated, covalent and noncovalent glucocorticoid receptor-steroid complexes from HTC cells

Comparison of DNA binding properties of activated, covalent and noncovalent glucocorticoid receptor-steroid complexes from HTC cells

Inhibition of estrous behavior in rats by intrahypothalamic application of agents that disrupt nuclear binding of estrogen-receptor complexes

Identification of a nucleic acid-regulated cyclic gmp-binding activity in Dictyostelium discoideum

Contact Info

Product

Resources

About