Boucher Philip E, Maris Ann E, Yang Mei-Shin, Stibitz Scott
Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, 8800 Rockville Pike, Bethesda, MD 20892, USA.
Mol Cell. 2003 Jan;11(1):163-73. doi: 10.1016/s1097-2765(03)00007-8.
Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding site to the -35 region. The orientation of BvgA monomers within the dimers is the same as that recently demonstrated by X-ray crystallographic methods for a dimer of the C-terminal domain of NarL bound to DNA. Use of FeBABE conjugates of RNAP alpha subunit C-terminal domain showed that binding of this domain is linearly coincident with binding of the BvgA dimers, but to a different helical face. These results reveal a previously undescribed mode of interaction between RNAP alpha-CTD and a transcriptional activator.
对FeBABE偶联的BvgA与百日咳博德特氏菌fha启动子结合的研究表明，由单体头对头缔合形成的三个二聚体从反向七联体初级结合位点到-35区域结合DNA螺旋的一个面。二聚体内BvgA单体的取向与最近通过X射线晶体学方法证明的与DNA结合的NarL C末端结构域二聚体的取向相同。使用RNA聚合酶α亚基C末端结构域的FeBABE偶联物表明，该结构域的结合与BvgA二聚体的结合呈线性重合，但结合到不同的螺旋面上。这些结果揭示了RNA聚合酶α-CTD与转录激活因子之间以前未描述的相互作用模式。
