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首页> 外文期刊>Biochemistry >Blue-light-induced unfolding of the Jα helix allows for the dimerization of aureochrome-LOV from the diatom Phaeodactylum tricornutum
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Blue-light-induced unfolding of the Jα helix allows for the dimerization of aureochrome-LOV from the diatom Phaeodactylum tricornutum

机译：蓝光诱导的Jα螺旋的展开允许来自硅藻Phaeodactylum tricornutum的aureochrome-LOV的二聚化

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摘要

Aureochromes have recently been shown to act as blue-light-regulated transcription factors in the stramenopile alga Vaucheria frigida. They comprise a light-, oxygen-, or voltage-sensitive (LOV) domain as a sensory module with flavin mononucleotide (FMN) as a chromophore and a basic region leucine zipper (bZIP) domain as an effector. Aureochromes are the only members of a large LOV protein family, where the effector domain is located N-terminal to the sensor domain. This domain inversion positions the linking Jα helix of other LOV proteins to the terminus, raising the question of the role of Jα in aureochrome signaling. In phototropins, signaling proceeds from LOV2 via dissociation and unwinding of the Jα helix to the C-terminal kinase effector domain. In contrast, other LOV proteins have been demonstrated to activate the effector without the unfolding of Jα. We investigated the LOV domain of aureochrome1a from the diatom Phaeodactylum tricornutum both with and without the Jα helix. Fourier transform infrared difference spectroscopy provides evidence that the Jα helix unfolds upon illumination. This unfolding is prerequisite for light-induced dimerization of LOV. Under illumination, full conversion to the dimer was observed by size exclusion chromatography. In the absence of the helix, a monomer was detected in the dark and in the light. As a further effect, the recovery of the dark state is 6-fold slower in LOV-Jα than LOV. We therefore postulate that the Jα helix plays an important role in aureochrome signaling.
机译：最近，已经证明了金黄色素能在拟南芥藻Vaucheria frigida中充当蓝光调节的转录因子。它们包括光，氧或电压敏感（LOV）域作为感觉模块，黄素单核苷酸（FMN）作为生色团和碱性区域亮氨酸拉链（bZIP）域作为效应子。金黄色素是大LOV蛋白家族的唯一成员，其中效应子结构域位于传感器结构域的N端。这种结构域倒置将其他LOV蛋白的Jα螺旋连接定位到末端，从而提出了Jα在金黄色素信号传导中的作用的问题。在光蛋白中，信号传导是通过LOV2通过Jα螺旋的解离和解旋到C末端激酶效应子结构域进行的。相反，已证明其他LOV蛋白可激活效应子而不释放Jα。我们研究了有和没有Jα螺旋的硅藻Phaeodactylum tricornutum的aureochrome1a的LOV域。傅里叶变换红外差光谱学提供了证据，表明Jα螺旋在照明后会展开。这种展开是光诱导的LOV二聚化的先决条件。在光照下，通过尺寸排阻色谱观察到完全转化为二聚体。在不存在螺旋的情况下，在黑暗和明亮的情况下都检测到单体。作为进一步的效果，LOV-Jα中暗态的恢复比LOV慢6倍。因此，我们假定Jα螺旋在金黄色素信号传导中起重要作用。

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