首页> 美国卫生研究院文献>The EMBO Journal >Characterization of SAF-A a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements.
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Characterization of SAF-A a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements.

机译:SAF-A的特征一种来自HeLa细胞的新型核DNA结合蛋白对核基质/支架附着DNA元素具有高亲和力。

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摘要

We identified four proteins in nuclear extracts from HeLa cells which specifically bind to a scaffold attachment region (SAR) element from the human genome. Of these four proteins, SAF-A (scaffold attachment factor A), shows the highest affinity for several homologous and heterologous SAR elements from vertebrate cells. SAF-A is an abundant nuclear protein and a constituent of the nuclear matrix and scaffold. The homogeneously purified protein is a novel double stranded DNA binding protein with an apparent molecular weight of 120 kDa. SAF-A binds at multiple sites to the human SAR element; competition studies with synthetic polynucleotides indicate that these sites most probably reside in the multitude of A/T-stretches which are distributed throughout this element. In addition we show by electron microscopy that the protein forms large aggregates and mediates the formation of looped DNA structures.
机译:我们从HeLa细胞的核提取物中鉴定出四种蛋白质,这些蛋白质与人基因组的支架附着区(SAR)元件特异性结合。在这四种蛋白质中,SAF-A(支架附着因子A)对脊椎动物细胞中的几种同源和异源SAR元素显示出最高的亲和力。 SAF-A是一种丰富的核蛋白,是核基质和支架的组成部分。均质纯化的蛋白质是表观分子量为120 kDa的新型双链DNA结合蛋白。 SAF-A在多个位点结合人类SAR元件;合成多核苷酸的竞争研究表明,这些位点最有可能位于分布在整个元件中的大量A / T拉伸中。此外,我们通过电子显微镜显示蛋白质形成大的聚集体并介导环状DNA结构的形成。

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