[Regulation of genetic activity by thyroid hormones. II. Specificity of interaction of cytoplasmic thyroxine receptor isolated from human embryonal fibroblasts and HeLa cells with DNA].
The work concerns a new approach to evaluating the receptor and hormone-receptor complex specific interaction with DNA and revealing the cause of the absence of the hormone-receptor complex acceptation with HeLa cell chromosomes. It has been shown that hormone-receptor complexing should precede specific interaction with DNA. The purified receptor-thyroxin complex is saturatable and specifically competes with Hae III restrictase, protecting specific sites of DNA recognition from this enzyme. Specificity of the hormone-receptor complex interaction with DNA depends on the sequences surrounding Hae III restriction site. The HeLa cell hormone-receptor complex does not interact with the recognition site for the normal hormone-receptor complex.
D002478:Cells, Cultured; D003593:Cytoplasm / Q000032:analysis; D004247:DNA / Q000032:analysis; D004622:Embryo, Mammalian; D005260:Female; D005347:Fibroblasts; D006367:HeLa Cells; D006801:Humans; D011247:Pregnancy; D011956:Receptors, Cell Surface / Q000235:genetics*; D013974:Thyroxine / Q000235:genetics*; D014178:Translocation, Genetic
D011956:Receptors, Cell Surface; D004247:DNA; D013974:Thyroxine
Reguliatsiia geneticheskoĭ aktivnosti tireoidnymi gormonami. II. Spetsifichnost' vzaĭmodeĭstviia tsitoplazmaticheskogo retseptora tiroksina iz fibroblastov embryona cheloveka i kletok HeLa s DNK.