A NOVEL DNA-BINDING MOTIF ABUTS THE ZINC FINGER DOMAIN OF INSECT NUCLEAR HORMONE RECEPTOR FTZ-F1 AND MOUSE EMBRYONAL LONG TERMINAL REPEAT-BINDING PROTEIN
A NOVEL DNA-BINDING MOTIF ABUTS THE ZINC FINGER DOMAIN OF INSECT NUCLEAR HORMONE RECEPTOR FTZ-F1 AND MOUSE EMBRYONAL LONG TERMINAL REPEAT-BINDING PROTEIN
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DOI：
10.1128/mcb.12.12.5667
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发表时间：
1992-12-01
影响因子：
5.3
通讯作者：
HIROSE, S
中科院分区：
文献类型：
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作者：
UEDA, H;SUN, GC;HIROSE, S
果蝇FTZ-F1、家蚕BmFTZ-F1和小鼠胚胎长末端重复序列结合蛋白是核激素受体超家族的成员，它们识别相同的序列5‘-PyCAAGG PyCPu-3’。在这些蛋白质中，紧邻锌指基序C末端的一个30个氨基酸组成的碱性区域是保守的，称为FTZ-F1盒。DNA结合区不同突变多肽的凝胶迁移率转移竞争表明，FTZ-F1盒和锌指基序参与了FTZ-F1与其靶点的高亲和力结合。利用凝胶迁移率移动矩阵竞争分析，我们证明FTZ-F1盒控制前三个碱基的识别，而锌指区域识别结合序列的其余部分。我们还发现FTZ-F1的DNA结合区以单体的形式识别并结合到DNA上。在核激素受体超家族的其他成员中出现FTZ-F1盒序列，可能表明这些受体构成了一个独特的亚家族，作为单体与DNA结合。
Fruit fly FTZ-F1, silkworm BmFTZ-F1, and mouse embryonal long terminal repeat-binding protein are members of the nuclear hormone receptor superfamily, which recognizes the same sequence, 5'-PyCAAGG PyCPu-3'. Among these proteins, a 30-amino-acid basic region abutting the C-terminal end of the zinc finger motif, designated the FTZ-F1 box, is conserved. Gel mobility shift competition by various mutant peptides of the DNA-binding region revealed that the FTZ-F1 box as well as the zinc finger motif is involved in the high-affinity binding of FTZ-F1 to its target site. Using a gel mobility shift matrix competition assay, we demonstrated that the FTZ-F1 box governs the recognition of the first three bases, while the zinc finger region recognizes the remaining part of the binding sequence. We also showed that the DNA-binding region of FTZ-F1 recognizes and binds to DNA as a monomer. Occurrence of the FTZ-F1 box sequence in other members of the nuclear hormone receptor superfamily raises the possibility that these receptors constitute a unique subfamily which binds to DNA as a monomer.