ABSTRACT:The tetrahydrocortisol-apolipoprotein A-I complex specifically interacts with eukaryotic DNA isolated from rat liver. This interaction is highly cooperative and of a saturating nature. One DNA molecule binds about 54 molecules of the complex. Smallangle X-ray scattering has shown that hydrogen bonds between nitrous bases are destroyed and that single-stranded structures are formed at the interaction of the tetrahydrocortisolapolipoprotein A-I complex with eukaryotic DNA. The most probable site of binding the tetrahydrocortisol-apolipoprotein A-I complex with DNA is the sequence of the CC(GCC) n type entering the structure of many genes, among them the structure of the human apolipoprotein A-I gene. Oligonucleotide of this type has been synthesized. The association constant (K ass ) of its complexation was shown to be 1.66 ⅐ 10 6 M
Ϫ1. Substitution of tetrahydrocortisol for cortisol in the complex results in a considerable decrease of K ass . IRspectroscopy study has shown that the interaction of tetrahydrocortisol with oligonucleotide CC(GCC) 3-5 is accompanied by the formation of hydrogen bonds via the CO-NH, PO 2 , and OH groups of desoxycytidinephosphate. The tetrahydrocortisol-apolipoprotein A-I complex alters the DNA secondary structure formed at the interaction with the hormone, causing the structural transition "order 3 tangle." It is assumed that in the GC-pairs of the given DNA sequence, tetrahydrocortisol initiates the rupture of hydrogen bonds, while the hydrophobic interactions between nitrous bases and apoA-I intensify this process.