首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The single Cys_2-His_2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding
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The single Cys_2-His_2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding

机译:GAGA蛋白的单个Cys_2-His_2锌指结构域侧翼为碱性残基,足以实现高亲和力的特异性DNA结合

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摘要

Specific DNA binding to the core consensus site GAGAGAG has been shown with an 82-residue peptide (residues 310-391) taken from the Drosophila transcription factor GAGA. Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) includes a single zinc finger of the Cys_2-His_2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger.
机译:已经显示出与核心共有位点GAGAGAG结合的特异性DNA,具有从果蝇转录因子GAGA提取的82个残基的肽段(残基310-391)。使用一系列缺失突变体,已证明特异性结合所需的最小结构域(残基310-372)包括Cys_2-His_2家族的单个锌指和位于其N末端的一段碱性氨基酸。锌指。

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