紧密结合型I12-X86乳糖阻遏物与非操纵子DNA的相互作用：复合物形成的盐依赖性
Interaction of the tight-binding I12-X86 lac repressor with non operator DNA: salt dependence of complex formation.
作者信息
Grebert P, Maurizot J C
出版信息
Nucleic Acids Res. 1986 Aug 26;14(16):6613-20. doi: 10.1093/nar/14.16.6613.
Abstract
The interaction of the wild-type lac repressor and its tight binding double mutant I12-X86 with a non operator-210 base pair-DNA fragment has been investigated using the nitrocellulose filter binding assay. While the affinity of the double mutant for this non specific DNA is increased as compared to that of the wild-type repressor, the number of ions released from the vicinity of the DNA upon complex formation is less important for the mutant than for the wild-type. These results demonstrate that the adaptation in the recognition surface of the repressor recently proposed by Mossing et al (J. Mol. Biol., 1985, 186, 295-305) in the case of an Oc mutant may be a more general phenomenon.
摘要
利用硝酸纤维素滤膜结合分析法，研究了野生型乳糖阻遏物及其紧密结合双突变体I12-X86与非操纵基因-210碱基对-DNA片段的相互作用。与野生型阻遏物相比，双突变体对这种非特异性DNA的亲和力有所增加，但与野生型相比，复合物形成时从DNA附近释放的离子数量对突变体来说不那么重要。这些结果表明，Mossing等人（《分子生物学杂志》，1985年，第186卷，第295 - 305页）最近提出的在Oc突变体情况下阻遏物识别表面的适应性变化可能是一种更普遍的现象。
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