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首页> 外文期刊>Nature structural biology >Structure of a HAP1--DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein
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Structure of a HAP1--DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein

机译：HAP1-DNA复合物的结构揭示了同二聚体蛋白的显着不对称DNA结合

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摘要

HAP1 is a member of a family of fungal transcription factors that contain a Zn sub(2)Cys sub(6) binuclear cluster domain and bind as homodimers to sequences containing two DNA half sites. We have determined the 2.5 Angstrom crystal structure of HAP1 bound to a cognate upstream activation sequence from the CYC7 gene. The structure reveals that HAP1 is bound in a dramatically asymmetric manner to the DNA target. This asymmetry aligns the Zn sub(2)Cys sub(6) domains in a tandem head-to-tail fashion to contact two DNA half sites, positions an N-terminal arm of one of the protein subunits to interact with the inter-half site base pairs in the DNA minor groove, and suggests a mechanism by which DNA-binding facilitates asymmetric dimerization by HAP1. Comparisons with the DNA complexes of the related GAL4, PPR1 and PUT3 proteins illustrate how a conserved protein domain can be reoriented to recognize DNA half sites of different polarities and how homodimeric proteins adopt dramatically asymmetric structures to recognize cognate DNA targets.
机译：HAP1是真菌转录因子家族的成员，该家族包含Zn sub（2）Cys sub（6）双核簇结构域，并作为同二聚体与包含两个DNA半位点的序列结合。我们已经确定HAP1的2.5埃晶体结构与CYC7基因的上游同源激活序列结合。该结构表明，HAP1以显着的不对称方式与DNA靶标结合。这种不对称性以头尾相接的方式对齐Zn sub（2）Cys sub（6）域，以接触两个DNA半位，定位其中一个蛋白亚基的N末端臂与半蛋白相互作用碱基对在DNA小沟中，并提出了一种DNA结合促进HAP1不对称二聚化的机制。与相关GAL4，PPR1和PUT3蛋白的DNA复合物的比较说明了如何重新定位保守的蛋白结构域以识别不同极性的DNA半位，以及同二聚体蛋白如何采用显着的不对称结构来识别同源的DNA靶标。

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