Binding of the estradiol-receptor complex to reconstituted nucleoacidic protein from calf uterus.
Non-histone protein-DNA complexes with acceptor activity for estradiol-receptor complexes were reconstituted from fractionated calf uterine chromatin. Acceptor activity had tissue specificity with target tissue binding exceeding non-target tissue binding. The binding of estradiol-receptor complexes to acceptor sites was dependent on intact non-histone protein-DNA complexes, reconstituted select non-histone proteins, and protein equivalent: DNA reconstitution ratios. [3H]Estradiol-receptor complexes were bound to reconstituted non-histone protein-DNA complexes (i.e., nucleoacidic protein) with a high affinity and with a limited number of binding sites. Fractionation of uterine chromatin non-histone proteins identified two major sets of non-histone proteins which had acceptor activity when reconstituted with DNA. Thus, it seems possible to reconstitute nucleoacidic protein fractions with specific acceptor activity for the calf uterine estrogen receptor.
D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004958:Estradiol / Q000378:metabolism; D005260:Female; D007700:Kinetics; D009698:Nucleoproteins / Q000378:metabolism*; D011189:Potassium Chloride / Q000494:pharmacology; D011402:Pronase; D011960:Receptors, Estrogen / Q000378:metabolism*; D014599:Uterus / Q000378:metabolism*
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D009698:Nucleoproteins; D011960:Receptors, Estrogen; D004958:Estradiol; D011189:Potassium Chloride; D011402:Pronase