Webster C, Merryweather A, Brammar W
ICI Joint Laboratory, University of Leicester, UK.
Mol Microbiol. 1992 Feb;6(3):371-7. doi: 10.1111/j.1365-2958.1992.tb01480.x.
Previous studies with purified variants of the 434 repressor having different operator-binding specificities have demonstrated the interactions of a heterodimeric repressor with a hybrid operator site. The present study investigates the interactions between the 434 repressor and its operator site. The optimum 434 operator half-site is used with a P22 operator half-site to create a hybrid 434/P22 operator. We show that this hybrid operator can be efficiently bound by a heterodimeric repressor, consisting of one wild-type 434 repressor monomer and one 434 repressor monomer with the binding specificity of the P22 repressor, to bring about repression in Escherichia coli.
先前对具有不同操纵子结合特异性的434阻遏物纯化变体进行的研究，已经证明了异二聚体阻遏物与杂交操纵子位点之间的相互作用。本研究调查了434阻遏物与其操纵子位点之间的相互作用。使用最佳的434操纵子半位点与P22操纵子半位点来创建一个杂交的434/P22操纵子。我们表明，这种杂交操纵子可以被一种异二聚体阻遏物有效结合，该异二聚体阻遏物由一个野生型434阻遏物单体和一个具有P22阻遏物结合特异性的434阻遏物单体组成，从而在大肠杆菌中实现抑制作用。
