Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex.
Protein-DNA interactions at recognition sites for the dioxin-Ah receptor complex.
复制标题
DOI：
--
复制
发表时间：
1989-10
期刊：
影响因子：
--
通讯作者：
M. Denison;J. Fisher;J. Whitlock
中科院分区：
文献类型：
--
作者：
M. Denison;J. Fisher;J. Whitlock
凝胶阻滞分析揭示了小鼠 CYP1A1 基因上游 700 个碱基对 DNA 结构域内配体 Ah 受体的六个结合位点簇。结合位点的核苷酸序列定义了配体受体的共有识别基序。共识主题不是对称的。共有基序的改变会导致受体-DNA 相互作用的减少。配体受体作为单体与其识别基序结合，并优先与双链 DNA 结合。这些观察结果揭示了 2,3,7,8-四氯二苯并-对二恶英和类固醇激素在各自作用机制上的明显差异。
Gel retardation analyses reveal a cluster of six binding sites for the liganded Ah receptor within a 700-base pair DNA domain upstream of the mouse CYP1A1 gene. The nucleotide sequences of the binding sites define a consensus recognition motif for the liganded receptor. The consensus motif is not symmetric. Alteration of the consensus motif produces a decrease in the receptor-DNA interaction. The ligand receptor binds as a monomer to its recognition motif and preferentially binds to double-stranded DNA. These observations reveal apparent differences between 2,3,7,8-tetrachlorodibenzo-p-dioxin and steroid hormones in their respective mechanisms of action.