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首页> 外文期刊>Biochemistry >Molecular Mechanism of Photozipper, a Light-Regulated Dimerizing Module Consisting of the bZIP and LOV Domains of Aureochrome-1
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Molecular Mechanism of Photozipper, a Light-Regulated Dimerizing Module Consisting of the bZIP and LOV Domains of Aureochrome-1

机译：光引象的分子机制，一种由无金色-1的Bzip和Lob结构域组成的光调节二聚化模块

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摘要

Aureochrome-1 (AUREO1) is a blue light (BL) receptor responsible for the BL-induced blanching of a stramenopile alga, Vaucheria frigida. The AUREO1 protein contains a central basic region/leucine zipper (bZIP) domain, and a C-terminal light-oxygen-voltage-sensing (LOV) domain. BL induces the dimerization of monomeric AUREO1, which subsequently increases the affinity of this transcription factor for its target DNA [Hisatomi, O., et al. (2014) J. Biol. Chem. 289, 17379-17391]. We constructed a synthetic gene encoding N-terminally truncated monomeric AUREO1 (designated Photozipper) to elucidate the molecular mechanism of this BL-regulated transcription factor and to develop it as an optogenetic tool. In this study, four different Photozipper (PZ) protein constructs were prepared comprising different N-terminal truncations. The monomer-dimer equilibria of the PZ constructs were investigated in the dark and light states. Dynamic light scattering and size-exclusion chromatography analyses revealed that the apparent dissociation constants of PZ dimers with and without the ZIP region were similar to 100 and 30 mu M, respectively, indicating that the ZIP region stabilized the monomeric form in the dark state. In the light state, fluorescence resonance energy transfer analyses demonstrated that deletion of the ZIP region increased the dissociation constant from similar to 0.15 to 0.6 mu M, suggesting that intermolecular LOV-LOV and ZIP-ZIP interactions stabilized the dimeric forms. Our results suggest that synergistic interactions between the LOV and bZIP domains stabilize the monomeric form in the dark state and the dimeric form in the light state, which possibly contributes to the function of PZ as a BL-regulated molecular switch.
机译：AUREOCHROME-1（AUROO1）是一种蓝光（BL）受体，其负责BL诱导的斯特拉络藻藻藻，VAUCHERIA Frigida的烫伤。 AURO1蛋白含有中央碱性区域/亮氨酸拉链（BZIP）结构域，以及C末端光 - 氧 - 电压传感（LOV）域。 Bl诱导单体AURO1的二聚化，其随后增加了该转录因子对其靶DNA的亲和力[Hisatomi，O.等。 （2014）J. Biol。化学。 289,17379-17391]。我们构建了编码N-末端截短的单体AUREO1（指定的光引象）的合成基因，以阐明该BL调节的转录因子的分子机制并使其作为致敏工具。在该研究中，制备包含不同N-末端截短的四种不同的光引象蛋白（PZ）蛋白质构建体。在黑暗和光源中研究了PZ构建体的单体二聚体平衡。动态光散射和尺寸排除色谱分析显示，具有和不具有ZIP区域的PZ二聚体的表观解离常数分别与100和30μm相似，表明ZIP区域稳定在黑暗状态下的单体形式。在光状态下，荧光共振能量转移分析表明，延伸区域的缺失增加了与0.15至0.6μm的解离常数增加，表明分子间热爱和Zip-Zip相互作用稳定了二聚体形式。我们的研究结果表明，LOV和BZIP结构域之间的协同相互作用在暗状态下稳定单体形式，并且在光状态下的二聚体形式稳定，这可能有助于PZ作为BL调节分子开关的功能。

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  • 来源
    《Biochemistry》 |2015年第21期|共12页
  • 作者

    Nakatani Yoichi; Hisatomi Osamu;

  • 作者单位

    Osaka Univ Grad Sch Sci Dept Earth &

    Space Sci Toyonaka Osaka 5600043 Japan;

    Osaka Univ Grad Sch Sci Dept Earth &

    Space Sci Toyonaka Osaka 5600043 Japan;

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  • 正文语种 eng
  • 中图分类 生物化学;
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