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The Drosophila P-element KP repressor protein dimerizes and interacts with multiple sites on P-element DNA.

机译:果蝇P元素KP阻遏蛋白使P元素DNA上的多个位点二聚化并相互作用。

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Drosophila P elements are mobile DNA elements that encode an 87-kDa transposase enzyme and transpositional repressor proteins. One of these repressor proteins is the 207-amino-acid KP protein which is encoded by a naturally occurring P element with an internal deletion. To study the molecular mechanisms by which KP represses transposition, the protein was expressed, purified, and characterized. We show that the KP protein binds to multiple sites on the ends of P-element DNA, unlike the full-length transposase protein. These sites include the high-affinity transposase binding site, an 11-bp transpositional enhancer, and, at the highest concentrations tested, the terminal 31-hp inverted repeats. The DNA binding domain was localized to the N-terminal 98 amino acids and contains a CCHC sequence, a potential metal binding motif. We also demonstrate that the KP repressor protein can dimerize and contains two protein-protein interaction regions and that this dimerization is essential for high-affinity DNA binding.
机译:果蝇P元件是可移动的DNA元件,可编码87 kDa的转座酶和转座阻遏蛋白。这些阻遏蛋白之一是207个氨基酸的KP蛋白,该蛋白由具有内部缺失的天然P元素编码。为了研究KP抑制转座的分子机制,该蛋白被表达,纯化和表征。我们表明,与全长转座酶蛋白不同,KP蛋白与P元素DNA末端的多个位点结合。这些位点包括高亲和力转座酶结合位点,11 bp的转座增强子,以及在最高测试浓度下的末端31 hp反向重复序列。 DNA结合结构域位于N端98个氨基酸处,并包含CCHC序列(潜在的金属结合基序)。我们还证明,KP阻遏蛋白可以二聚化并包含两个蛋白质-蛋白质相互作用区域,并且这种二聚化对于高亲和力DNA结合至关重要。

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