The Polynucleotide Binding Sites of Estradiol Receptor Complexes

Dickerman, Herbert W.; Kumar, Salil

doi:10.1007/978-1-4615-7192-6_1

Cited by 5 publications

(1 citation statement)

References 32 publications

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“…The oligodeoxynucleotides are, of course, limited probes for exploring the polynucleotide domains of steroid receptors, as they do not mimic the complete three-dimensional array of a DNA helix binding site. In fact, the avidity for oligo(dG)-cellulose may reflect a feature of holoreceptor binding to abortive rather than effective nuclear sites [22]. But they do afford a means of assessing nucleotide recognition by steroid holoreceptors and those factors, ie, inhibitors, accessory proteins, etc, which modulate this recognition.…”

Section: Jcb:27mentioning

confidence: 99%

Oligodeoxynucleotide base recognition by steroid hormone receptors

Kumar

Beach

Dickerman

1983

J of Cellular Biochemistry

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Oligodeoxynucleotides covalently linked to cellulose were used as probes of the DNA-binding domains of mouse steroid holoreceptors. With uterine cytosol estrogen receptor (E2R) the relative binding order, in prior studies, was oligo(dG) greater than oligo(dT) greater than or equal to oligo(dC) much greater than oligo(dA) greater than oligo(dI). The binding reactions were salt-sensitive with an optimal KCl concentration of 0.1-0.2 M. There was no enhancement of binding by activation, either temperature- or salt-induced. In the present study, using the oligomer ligands at a lower concentration, oligo(dT) binding was greater than that to oligo(dC). Quantitative differences in oligodeoxynucleotide binding were elicited by a number of inhibitors. These differences are again seen by exposure of E2R to chaotropic salts such as SCN-, ClO-4 and NO3- as well as to putative modifiers of receptor amino acids, ie, iodoacetamide, 1,2 cyclohexanedione, and Rose Bengal. These results, and the quantitative differences following heat and purification, led to a designation of two types of subsites within the DNA-binding domain of uterine E2R. These are stable G sites, which interact with oligo(dG); and labile N sites, which bind to oligo(dT), oligo(dC) and oligo(dA). Stimulation of binding to N sites and stabilization of the holoreceptor was effected by histones H2A and H2B. However, the differential response to incubation at 37 degrees C was not altered by addition of H2B. Treatment of uterine E2R by limited proteolysis also eliminated the stimulatory response to H2B. The above data, as well as prior studies, indicate that steroid holoreceptors can discriminate between the structural features of deoxynucleotide bases and this recognition process can be modulated by accessory proteins.

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Section: Jcb:27mentioning

confidence: 99%