Thanki K H, Beach T A, Dickerman H W
J Biol Chem. 1978 Nov 10;253(21):7744-50.
As a model for the nonspecific interaction of steroid receptors with DNA, the binding of estradiol.receptor complexes of mouse kidney and uterine cytosols to oligo(dT)-cellulose was studied in detail. A limited concentration range of monovalent cationic salts was required for optimal binding, regardless of prior activation of the receptor complexes or the oligomer ligand. Thermal activation of the receptor complexes did not facilitate binding. The reaction was selective for intracellular steroid hormone.receptor complexes, as extracellular proteins binding estradiol with low affinity (bovine serum albumin) or high affinity (mouse alpha-fetoprotein) were inactive. Both crude and partially purified kidney cytosol receptor complexes bound preferentially to oligo(dT)- and oligo(dC)-celluloses, rather than oligo(dA)-celluloses. These findings suggest that at least part of the nonspecific interaction of estradiol.receptor complexes with native DNA is through a salt-sensitive binding of the complex to pyrimidine-rich surfaces of the DNA.
作为类固醇受体与DNA非特异性相互作用的模型，对小鼠肾脏和子宫胞质溶胶中的雌二醇-受体复合物与寡聚（dT）-纤维素的结合进行了详细研究。无论受体复合物或寡聚体配体事先是否被激活，都需要有限浓度范围的单价阳离子盐来实现最佳结合。受体复合物的热激活并不能促进结合。该反应对细胞内类固醇激素-受体复合物具有选择性，因为与雌二醇结合亲和力低（牛血清白蛋白）或高亲和力（小鼠甲胎蛋白）的细胞外蛋白质没有活性。粗制的和部分纯化的肾脏胞质溶胶受体复合物都优先与寡聚（dT）-纤维素和寡聚（dC）-纤维素结合，而不是与寡聚（dA）-纤维素结合。这些发现表明，雌二醇-受体复合物与天然DNA的非特异性相互作用至少部分是通过复合物与DNA富含嘧啶表面的盐敏感结合实现的。
