Effect of pyridoxal 5'-phosphate on oligodeoxynucleotide binding of mouse uterine cytosol estradiol-receptor complexes.
Pyridoxal-5'-phosphate, an inhibitor of DNA binding of glucocorticoid-, progesterone-, and estrogen-receptor complexes, also blocks the interaction of mouse uterine cytosol estradiol-receptor complexes with oligodeoxynucleotides covalently linked to celluloses. Other derivatives of pyridoxine were ineffective. The inhibition was irreversible only after borohydride reduction. Experiments with three oligodeoxynucleotides showed a 4-fold range of differences in the pyridoxal-5'-phosphate concentrations needed to inhibit 50% of the binding: oligo(dG)-cellulose, 3.1 mM; oligo(dT)-cellulose, 1.5 mM; and oligo(dC)-cellulose, 0.8 mM. Inhibition of binding occurred more rapidly with the oligodeoxypyrimidines than with oligo(dG)-cellulose. Pyridoxal-5'-phosphate was competitive with the oligodeoxynucleotides in its mode of inhibition, suggesting the polynucleotide-binding domain as a site of action. These data indicate a microheterogeneity of oligodeoxynucleotide-binding sites in the estradiol-receptor complex which is reflected in sensitivity to pyridoxal-5'-phosphate.
D000596:Amino Acids / Q000494:pharmacology; D000818:Animals; D002846:Chromatography, Affinity; D003600:Cytosol / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism*; D005260:Female; D007700:Kinetics; D051379:Mice; D008815:Mice, Inbred Strains; D009838:Oligodeoxyribonucleotides / Q000378:metabolism*; D009841:Oligonucleotides / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000494:pharmacology*; D011959:Receptors, Estradiol; D011960:Receptors, Estrogen / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D014599:Uterus / Q000378:metabolism*
D000596:Amino Acids; D009838:Oligodeoxyribonucleotides; D009841:Oligonucleotides; D011959:Receptors, Estradiol; D011960:Receptors, Estrogen; D004958:Estradiol; D011732:Pyridoxal Phosphate