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首页> 外文期刊>Journal of Molecular Biology >A DNA mimic: The structure and mechanism of action for the anti-repressor protein AbbA
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A DNA mimic: The structure and mechanism of action for the anti-repressor protein AbbA

机译：DNA模拟：抗阻遏蛋白AbbA的结构和作用机理

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摘要

Bacteria respond to adverse environmental conditions by switching on the expression of large numbers of genes that enable them to adapt to unfavorable circumstances. In Bacillus subtilis, many adaptive genes are under the negative control of the global transition state regulator, the repressor protein AbrB. Stressful conditions lead to the de-repression of genes under AbrB control. Contributing to this de-repression is AbbA, an anti-repressor that binds to and blocks AbrB from binding to DNA. Here, we have determined the NMR structure of the functional AbbA dimer, confirmed that it binds to the N-terminal DNA-binding domain of AbrB, and have provided an initial description for the interaction using computational docking procedures. Interestingly, we show that AbbA has structural and surface characteristics that closely mimic the DNA phosphate backbone, enabling it to readily carry out its physiological function.
机译：细菌通过开启大量基因的表达来应对不利的环境条件，这些基因使它们能够适应不利的环境。在枯草芽孢杆菌中，许多适应性基因处于全局过渡状态调节剂阻遏蛋白AbrB的负调控下。压力条件导致在AbrB控制下基因的抑制。造成这种抑制的因素是AbbA，它是一种抗阻遏物，与AbrB结合并阻止其与DNA结合。在这里，我们确定了功能性AbbA二聚体的NMR结构，证实它与AbrB的N端DNA结合域结合，并使用计算对接程序为相互作用提供了初步说明。有趣的是，我们表明AbbA具有紧密模仿DNA磷酸骨架的结构和表面特征，使其能够轻松实现其生理功能。

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