REPRESSOR AND ANTIREPRESSOR PROTEINS OF BACTERIOPHAGE

目的是了解蛋白质如何识别特定的 双链DNA序列，并了解如何 基因调控蛋白的活性由 与其他蛋白质的相互作用。 遗传学，生物化学， 结构研究将用于阐明详细的 噬菌体的Arc和Mnt阻遏物 P22与它们各自的操纵子序列结合，并且与 表征增强或改变结合的突变 λ阻遏物和λ Cro蛋白的特异性。 消除或增强合作相互作用的突变 在与相邻操纵子结合的λ阻遏物分子之间 位点也将被分离，这些突变对 蛋白质介导的DNA环和线性聚合 将确定溶液中的阻遏物。 最后，机制 RecA介导的和P22抗阻遏物介导的失活 λ阻遏物将通过研究生物化学 突变蛋白质的性质，显示改变的性质， 失活反应。

The objective is to understand how proteins recognize specific sequences of double stranded DNA and to understand how the activities of gene regulatory proteins are controlled by interactions with other proteins. Genetic, biochemical, and structural studies will be used to elucidate the detailed mechanism by which the Arc and Mnt repressors of bacteriophage P22 bind to their respective operator sequences, and to characterize mutations that enhance or alter the binding specificity of the lambda repressor and lambda Cro proteins. Mutations that abolish or enhance cooperative interactions between lambda repressor molecules bound at adjacent operator sites will also be isolated, and the effects of these mutations on protein-mediated DNA looping and the linear polymerization of repressor in solution will be determined. Finally, the mechanisms of RecA-mediated and P22 antirepressor-mediated inactivation of lambda repressor will be explored by studying the biochemical properties of mutant proteins that display altered properties in the inactivation reactions.