Coy M
Chemical Biodynamics, University of California, Berkeley 94720, USA.
Biochem Biophys Res Commun. 1995 Jul 26;212(3):784-92. doi: 10.1006/bbrc.1995.2037.
The interaction of the Ferric Uptake Regulation (Fur) protein with the backbone of operator DNA was analyzed by hydroxyl radical footprinting and the ethylation interference assay. Comparison of the contacts made by Fur and those made by proteins containing the helix-turn-helix or related motifs shows that the mode of DNA binding by this repressor is unique. Ethylation interference experiments demonstrate that there are relatively few phosphate contacts of unique disposition while hydroxyl radical footprinting demonstrates that Fur-operator contacts are segregated on one face of the helix and span nearly three successive major grooves.
通过羟基自由基足迹法和乙基化干扰试验分析了铁摄取调节（Fur）蛋白与操纵基因DNA骨架的相互作用。对Fur形成的接触与含有螺旋-转角-螺旋或相关基序的蛋白质形成的接触进行比较，结果表明这种阻遏物的DNA结合模式是独特的。乙基化干扰实验表明，具有独特排列的磷酸接触相对较少，而羟基自由基足迹法表明Fur-操纵基因的接触集中在螺旋的一个面上，跨越了近三个连续的大沟。
