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A network of specific minor-groove contacts is a common characteristic of paired-domain-DNA interactions.

机译:特定的小沟槽接触网络是成对域DNA相互作用的共同特征。

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摘要

Pax proteins are a family of transcription factors conserved during evolution and able to bind specific DNA sequences through a domain called a "paired domain'. The DNA-binding specificity of the Pax-8 paired domain was investigated. Site-selection experiments indicate that Pax-8 binds to a consensus sequence similar to those bound by Pax-2 and Pax-5. When consensus sequences of various paired domains are observed in light of recent structural studies describing paired-domain-DNA interaction [Xu, Rould, Jun, Desplan and Pabo (1995) Cell 80, 639-650], it appears that base-pairs contacted in the minor groove are conserved, while most of the base-pairs contacted in the major groove are not. Therefore a network of specific minor groove contacts is a common characteristic of paired-domain-DNA interactions. The functional importance of such a network was successfully tested by analysing the effect of consensus-based mutations on the Pax-8 binding site of the thyroglobulin promoter.
机译:Pax蛋白是在进化过程中保守的转录因子家族,能够通过称为“配对域”的结构域结合特定的DNA序列,研究了Pax-8配对结构域的DNA结合特异性,位点选择实验表明Pax -8结合到与Pax-2和Pax-5结合的共有序列相似的序列。当根据描述成对域-DNA相互作用的最新结构研究观察到各种成对结构域的共有序列时[Xu,Rould,Jun,Desplan和Pabo(1995)Cell 80,639-650],似乎在小沟中接触的碱基对是保守的,而在主沟中接触的大多数碱基对却不保守,因此特定的小沟接触网络是配对域DNA相互作用的共同特征,通过分析基于共识的突变对甲状腺球蛋白启动子Pax-8结合位点的影响,成功测试了这种网络的功能重要性。

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