Schmitz A, Galas D J
Nucleic Acids Res. 1980 Feb 11;8(3):487-506. doi: 10.1093/nar/8.3.487.
The tight-binding I12-X86 lac repressor binds to non-operator DNA in a sequence-specific fashion. Using the DNA of the E. coli I gene we have investigated these sequence-specific interactions and compared them to the operator binding of wild-type repressor. The specific, non-operator DNA interactions are sensitive to the inducer IPTG. One strong binding site in the I gene DNA was found to be one of two expected on the basis of their homology with the lac operator. The binding of I12-X86 repressor to this site was visualized using the footprinting technique, and found to be consistent with an operator-like binding configuration. The protection pattern extends into an adjacent sequence suggesting that two repressor tetramers are bound in tandem.
紧密结合的I12-X86乳糖阻遏物以序列特异性方式与非操纵子DNA结合。利用大肠杆菌I基因的DNA,我们研究了这些序列特异性相互作用,并将其与野生型阻遏物的操纵子结合进行了比较。特异性的非操纵子DNA相互作用对诱导剂IPTG敏感。在I基因DNA中发现的一个强结合位点是基于其与乳糖操纵子的同源性所预期的两个位点之一。使用足迹技术观察到I12-X86阻遏物与该位点的结合,发现其与类似操纵子的结合构型一致。保护模式延伸到相邻序列,表明两个阻遏物四聚体串联结合。