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首页> 外文期刊>Molecular cell >The Response Regulator BvgA and RNA Polymerase alpha Subunit C-Terminal Domain Bind Simultaneously to Different Faces of the Same Segment of Promoter DNA.
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The Response Regulator BvgA and RNA Polymerase alpha Subunit C-Terminal Domain Bind Simultaneously to Different Faces of the Same Segment of Promoter DNA.

机译:响应调节剂BvgA和RNA聚合酶α亚基C末端域同时绑定到启动子DNA同一段的不同面孔。

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摘要

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.
机译:FeBABE缀合的BvgA与百日咳博德特氏菌的fha启动子的结合研究表明,由单体的头对头结合形成的三个二聚体将DNA螺旋的一个面从倒七联的初级结合位点结合到了螺旋藻上。 -35地区。 BvgA单体在二聚体中的取向与最近通过X射线晶体学方法证明与DNA结合的NarL C端结构域的二聚体的取向相同。使用RNA聚合酶α亚基C末端结构域的FeBABE共轭物显示,该结构域的结合与BvgA二聚体的结合线性一致,但结合到不同的螺旋面上。这些结果揭示了RNAPα-CTD和转录激活因子之间以前未描述的相互作用方式。

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