Gang J B, Harman J G
Department of Chemistry, Kyungwon University, Sungnam, Korea.
Mol Cells. 1997 Jun 30;7(3):444-7.
Changes in DNA structure induced by cAMP receptor protein (CRP) binding to the lac-control region contained on a 231 bp fragment were investigated by measurement of the molar cyclization factor (jM). Increases in jM were observed at low to moderate CRP: cAMP complex concentrations and correlated with CRP binding to the promoter-proximal CRP binding site. At CRP:cAMP complex concentrations greater than 200 nM, decreases in jM correlated with CRP binding to both the promoter-proximal and the operator-proximal CRP binding sites. These results show that binding of the CRP:cAMP complex to the operator-proximal CRP binding site induces a structural change in lac DNA.
通过测量摩尔环化因子(jM),研究了环磷酸腺苷受体蛋白(CRP)与包含在231 bp片段上的乳糖操纵子控制区域结合所诱导的DNA结构变化。在低至中等CRP:cAMP复合物浓度下观察到jM增加,且与CRP结合到启动子近端CRP结合位点相关。在CRP:cAMP复合物浓度大于200 nM时,jM降低与CRP结合到启动子近端和操纵基因近端CRP结合位点均相关。这些结果表明,CRP:cAMP复合物与操纵基因近端CRP结合位点的结合诱导了乳糖操纵子DNA的结构变化。