Specificity of oligodeoxynucleotide binding of mouse uterine cytosol estradiol receptors.

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Abstract
The relative capacities of oligodeoxynucleotides, covalently linked to cellulose, to bind estradiol receptor complexes (E2R) of mouse uterine cytosol have been shown to follow the order oligo(dG) > oligo(dT) greater than or equal to oligo(dC) > oligo(dA). The E2R . oligo(dT)-cellulose-binding reaction is more sensitive to Cibacron blue F3GA than is E2R . oligo(dG)-cellulose or oligo(dC)-cellulose binding. Preformed E2R . oligo(dT)- or oligo(dC)-cellulose complexes are dissociated more readily by lower concentrations of KCl or Cibacron blue F3GA than is the E2R . oligo(dG)-cellulose complex. Preincubation of E2R at 37 degrees C results in a rapid loss of binding ability towards oligo(dT)- and oligo(dC)-cellulose, while up to 90% of the binding ability to oligo(dG)-cellulose is retained. On the basis of the differential sensitivities of E2R to temperature and the inhibition by Cibacron blue F3GA of the binding reaction, it is suggested that the polynucleotide-binding domain consists of two types of subsites, one of which has a higher affinity for oligo(dG) residues and the other of which recognizes oligo(dT), oligo(dC), and, to a lesser extent, oligo(dA).