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几乎所有已研究过的Cys_2 His_2锌指蛋白质在体外都有与特定序列的DNA结合的活性,本文进一步研究了它们和其它种类的核酸结合的可能性。 转录因子Spl是一个具有锌指结构的DNA结合蛋白质,用它和DNA-RNA杂种分子结合。实验结果表明:Spl和19bp的DNA双链在一定的条件下结合,表观解离常数为40nM,DNA-RNA杂种分子(DNA链富含G)与Spl有相似强度的结合,并且是富含G的DNA链与Spl结合。相反,DNA-RNA杂种分子(RNA链富含G)和 RNA-RNA双链分子与Spl的结合强度分别只有前者的1/10和1/100。
Almost all of the Cys_2 His_2 zinc finger proteins that have been studied have the activity of binding to DNA of a specific sequence in vitro and the possibility of their binding to other kinds of nucleic acids is further studied in this paper. The transcription factor Spl is a DNA-binding protein with a zinc-finger structure that binds to DNA-RNA hybrids. The experimental results show that Spl and 19bp DNA duplexes bind under certain conditions, the apparent dissociation constant is 40nM, DNA-RNA hybrids (DNA chain is rich in G) and Spl have similar intensity of binding, and is rich in The DNA strand of G binds to Spl. In contrast, the binding strength of DNA-RNA hybrids (RNA-rich G) and RNA-RNA double-stranded molecules to Spl was only 1/10 and 1/100 of the former, respectively.