Abstract
The in vitro effect of tetrahydrocortisol-apolipoprotein A-I complex on native adult rat liver DNA results in the formation of S1 nuclease sensitive fragments that are irregularly distributed throughout a genome. Low-angle X-ray scattering showed that after the interaction with the tetrahydrocortisol-apolipoprotein A-I complex, DNA can bind to RNA-polymerase with a high and dose-dependent cooperativity. This indicates that the effect of tetrahydrocortisol-apolipoprotein A-I complex on secondary eukaryotic DNA structure causes a local denaturation of the double helix, promoting high cooperativity of binding to RNA-polymerase. The reduced form of the hormone, tetrahydrocortisol, previously considered as an inactive metabolite, when complexed with apolipoprotein A-I, promotes a biological function similar to that of a transcription factor.
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