Kim Y I, Hu J C
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128, USA.
Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7510-4. doi: 10.1073/pnas.92.16.7510.
The first 6 amino acids (NH2-Ser1-Thr2-Lys3-Lys4-Lys5-Pro6) of bacteriophage lambda cI repressor form a flexible arm that wraps around the operator DNA. Homodimeric lambda repressor has two arms. To determine whether both arms are necessary or only one arm is sufficient for operator binding, we constructed heterodimeric repressors with two, one, or no arms by fusing the DNA binding domain of lambda repressor to leucine zippers from Fos and Jun. Although only one arm is visible in the cocrystal structure of the N-domain-operator complex, our results indicate that both arms are required for optimal operator binding and normal site discrimination.
噬菌体λ cI 阻遏蛋白的前6个氨基酸(NH2-Ser1-Thr2-Lys3-Lys4-Lys5-Pro6)形成一个柔性臂,该臂环绕操纵基因DNA。同二聚体λ阻遏蛋白有两个臂。为了确定两个臂对于操纵基因结合是否都是必需的,还是只有一个臂就足够了,我们通过将λ阻遏蛋白的DNA结合结构域与来自Fos和Jun的亮氨酸拉链融合,构建了具有两个臂、一个臂或没有臂的异二聚体阻遏蛋白。尽管在N结构域-操纵基因复合物的共晶体结构中只可见一个臂,但我们的结果表明,两个臂对于最佳的操纵基因结合和正常的位点识别都是必需的。