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首页> 外文期刊>Nucleic Acids Research >Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2)
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Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2)

机译：TetR家族蛋白CprB从天蓝色链霉菌A3（2）转录调控的结构和功能基础。

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摘要

Antibiotic production and resistance pathways in Streptomyces are dictated by the interplay of transcriptional regulatory proteins that trigger downstream responses via binding to small diffusible molecules. To decipher the mode of DNA binding and the associated allosteric mechanism in the subclass of transcription factors that are induced by gamma-butyrolactones, we present the crystal structure of CprB in complex with the consensus DNA element to a resolution of 3.25 angstrom. Binding of the DNA results in the restructuring of the dimeric interface of CprB, inducing a pendulum-like motion of the helix-turn-helix motif that inserts into the major groove. The crystal structure revealed that, CprB is bound to DNA as a dimer of dimers with the mode of binding being analogous to the broad spectrum multidrug transporter protein QacR from the antibiotic resistant strain Staphylococcus aureus. It was demonstrated that the CprB displays a cooperative mode of DNA binding, following a clamp and click model. Experiments performed on a subset of DNA sequences from Streptomyces coelicolor A3(2) suggest that CprB is most likely a pleiotropic regulator. Apart from serving as an autoregulator, it is potentially a part of a network of proteins that modulates the gamma-butyrolactone synthesis and antibiotic regulation pathways in S. coelicolor A3(2).
机译：链霉菌中的抗生素产生和耐药途径取决于转录调节蛋白的相互作用，这些转录调节蛋白通过与小的可扩散分子结合而触发下游反应。为了解释由γ-丁内酯诱导的转录因子亚类中DNA结合的模式和相关的变构机制，我们提出了CprB的晶体结构，与共有DNA元件复合，分辨率为3.25埃。 DNA的结合导致CprB的二聚体界面的重组，从而引起插入主沟的螺旋-转-螺旋基序的钟摆状运动。晶体结构表明，CprB以二聚体的二聚体形式与DNA结合，其结合方式类似于来自抗生素抗性金黄色葡萄球菌的广谱多药转运蛋白QacR。证明了CprB遵循钳和点击模型显示了DNA结合的合作模式。对来自天蓝色链霉菌A3（2）的DNA序列的子集进行的实验表明，CprB最有可能是多效性调节剂。除了充当自动调节器之外，它还可能是蛋白质网络的一部分，该蛋白质可以调节天蓝色链霉菌A3（2）中的γ-丁内酯合成和抗生素调节途径。

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