Influence of inorganic cations and histone proteins on the terbium(III)-nucleic acid interaction.
We have studied the interaction of the fluorescent lanthanide, terbium(III) (Tb3+), with polynucleotides and linear and superhelical DNA, through employment of mono- and multivalent cations as competitive inhibitors. Increasingly effective competitive inhibiton of the Tb3+-nucleic acid interaction was achieved, for the most part, in the cation order monovalent less than divalent less than tetravalent. The divalent cation Cu2+ proved to be an exception to this trend, and was the strongest competitive inhibitor or all cations tested, exhibiting an affinity for Tb3+ binding sites over twice that of Tb3+ itself. Unexpectedly, a narrow range of low sodium ion concentration (8--20 mM) was found to be effective in inducing localized unwinding or unstacking of linear and supercoiled DNA double helices, a phenomenon detectable through the use of both Tb3+ fluorescence enhancement and ultraviolet spectroscopy. Within a similar range of low sodium ion concentration, moreover, histone H1 was substantially more effective in displacing terbium ion from DNA than either histones H2B or H4, but at higher ionic strength, this difference was absent. These results further confirm the sensitivity and specificity of Tb3+ as a conformational probe of nucleic acids.
D000818:Animals; D002412:Cations / Q000494:pharmacology*; D002417:Cattle; D002645:Chickens; D003300:Copper / Q000494:pharmacology; D004247:DNA / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000378:metabolism*; D006657:Histones / Q000494:pharmacology*; D009690:Nucleic Acid Conformation / Q000187:drug effects; D011131:Polyribonucleotides / Q000378:metabolism*; D012964:Sodium / Q000494:pharmacology; D013725:Terbium / Q000378:metabolism*
D002412:Cations; D005456:Fluorescent Dyes; D006657:Histones; D011131:Polyribonucleotides; D013725:Terbium; D003300:Copper; D004247:DNA; D012964:Sodium