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首页> 外文期刊>Journal of Molecular Biology >Light-induced differences in conformational dynamics of the circadian clock regulator VIVID
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Light-induced differences in conformational dynamics of the circadian clock regulator VIVID

机译：光诱导的昼夜节律调节器VIVID的构象动力学差异

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摘要

The LOV (light-oxygen-voltage) domain protein VIVID (VVD) is a negative regulator of the circadian transcription factor White Collar Complex and controls light response and photoadaptation in Neurospora. Blue light converts VIVID from the dark state into the light state (VVDL) with concomitant homodimerization. Upon return to low-light conditions, VVD very slowly reverts back into the monomeric dark state (VVDD). To better understand the nature of the conformational changes that are the basis for the light-dark switch in VVD, we used hydrogen exchange mass spectrometry to probe solvent accessibility of backbone amide protons. Our data demonstrate that all structural elements of VVDD except for the N-cap region exchange according to the rare EX1 mechanism indicating a reversible unfolding with rather slow refolding rate. Interestingly, the unfolding halftimes of different elements were not identical but varied from 400 to 900 s. VVDL also exchanges according to the EX1 mechanism, albeit with a halftime of 6 h. Surprisingly, the dimerization interface showed very little protection suggesting a rapid dimer-monomer interconversion.
机译：LOV（光-氧-电压）域蛋白VIVID（VVD）是昼夜节律转录因子白领复合体的负调节剂，可控制神经孢菌中的光响应和光适应性。蓝光伴随同质二聚化，将VIVID从暗状态转换为亮状态（VVDL）。返回到弱光条件后，VVD会非常缓慢地恢复为单体暗态（VVDD）。为了更好地了解作为VVD中明暗转换基础的构象变化的性质，我们使用了氢交换质谱法来检测骨架酰胺质子的溶剂可及性。我们的数据表明，根据稀有的EX1机制，除N-cap区域外，VVDD的所有结构元素均以可逆的展开速率和相当缓慢的折叠速率进行交换。有趣的是，不同元素的展开半衰期并不相同，而是在400到900 s之间变化。 VVDL也根据EX1机制进行交换，尽管半场时间为6小时。出乎意料的是，二聚化界面显示出很少的保护，表明快速的二聚体-单体相互转化。

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