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首页> 外文期刊>Journal of Molecular Biology >The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study.
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The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study.

机译：不会翻转的开关：来自枯草芽孢杆菌的蓝光受体YtvA采用细长的二聚体构象，而与激活状态无关，这通过AUC和SAXS联合研究显示。

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摘要

Photoreceptors play an important role in plants and bacteria by converting extracellular stimuli into intracellular signals. One distinct class are the blue-light-sensitive phototropins harboring a light-oxygen-voltage (LOV) domain coupled to various effector domains. Photon absorption by the chromophore within the LOV domain results in an activation of the output domain via mechanisms that are hitherto not well understood. The photoreceptor YtvA from Bacillus subtilis is a bacterial analog of phototropins, consists of an LOV and a sulfate transporter/anti-sigma factor antagonist domain, and is involved in the response of the bacterium to environmental stress. We present here analytical ultracentrifugation studies and small-angle X-ray scattering experiments, showing that YtvA is a dimer. On the basis of these results, we present a low-resolution model of the dimer in the dark and the lit state of the protein. In addition, we show that YtvA does not change its oligomerization state or its overall shape upon light activation.
机译：感光细胞通过将细胞外刺激转化为细胞内信号，在植物和细菌中发挥重要作用。一类独特的是对光敏感的蓝色光敏性光蛋白，它具有耦合到各种效应子域的光氧电压（LOV）域。 LOV域内的生色团对光子的吸收会导致通过迄今尚未很好理解的机制激活输出域。枯草芽孢杆菌的光感受器YtvA是光蛋白的细菌类似物，由LOV和硫酸盐转运蛋白/抗-sigma因子拮抗剂域组成，并参与细菌对环境胁迫的反应。我们在这里介绍分析超速离心研究和小角度X射线散射实验，表明YtvA是二聚体。基于这些结果，我们提出了蛋白质在黑暗和光照状态下二聚体的低分辨率模型。此外，我们显示YtvA不会在光激活后改变其低聚状态或整体形状。

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