Diverse Responses to Blue Light via LOV Photoreseptors
Diverse Responses to Blue Light via LOV Photoreseptors
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LOV 光感受器对蓝光的不同反应
DOI：
10.1093/pcp/pcs172
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发表时间：
2013
期刊：
影响因子：
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通讯作者：
Shimazaki K and Tokutomi S
中科院分区：
文献类型：
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作者：
M.Asada;Shimazaki K and Tokutomi S
植物利用光不仅作为光合作用的能量来源，而且作为指导许多发育和生理过程的环境线索。为此，植物进化出了两种主要类型的光感受器：光敏色素（Franklin and Quail 2010），它们感知红光/远红光；以及紫外线(UV)-A/蓝光（BL）感应光感受器，其中包括隐花色素（Liu et al. 2011）、趋光素（Christie 2007）和下面描述的其他BL受体。此外，最近发现了第三类UV-B受体UVR8 （Rizzini et al. 2011）。BL受体研究的悠久历史可以追溯到著名的查尔斯·达尔文最初的观察，他发现植物能够向光移动（达尔文和达尔文1881）。长期以来，BL受体中的发色团是黄素还是类胡萝卜素一直存在争议（Senger 1980）。这一问题通过第一个BL受体的鉴定得到了部分解决，该受体对应于一种名为cryptochrome的黄素蛋白（Ahmad and Cashmore 1993）。在这一发现之后不久，Briggs小组证明，拟南芥非嗜光性下胚轴1 （nph1）突变体中被破坏的基因编码了一个嗜光性反应所需的BL受体（Huala et al. 1997, Christie et al. 1998）。NPH1的同源物NON-PHOTOTROPIC HYPOCOTYL-LIKE 1 （NPL1）很快被发现（Kagawa et al. 2001）；此后，NPH1和NPL1分别更名为致光蛋白1 （phot1）和phot2。光促素介导多种植物反应，如叶绿体重新定位运动（Kagawa等，2001年，Sakai等，2001年）、气孔打开（Kinoshita等，2001年）、早期下轴生长抑制（Folta和Spaulding 2001年）、叶片变平（Sakamoto和Briggs 2002年）、叶片定位（Inoue等，2005年）、核定位（Iwabuchi等，2007年，Tsuboi等，2007年）、太阳跟踪（Inoue等，2008b）和叶片光形态形成（Kozuka等，2011年）。其中phot1在宽光强范围内工作，而phot2作为高光传感器。这些生理反应通过增加对光和二氧化碳的吸收来促进植物的光合作用（Takemiya et al. 2005）。除了这两种光促性蛋白外，在拟南芥中还发现了一个BL受体家族蛋白，其特征是包含一个光、氧或电压（LOV）结构域、一个F-box和一个Kelch重复序列。这些蛋白包括ZEITLUPE （ZTL）、FLAVIN-BINDING KELCH REPEAT F-BOX 1 （FKF1）和LOV KELCH PROTEIN 2 (LKP2)，它们被认为通过控制bl依赖性蛋白降解来调节生物钟和光周期开花（Ito et al. 2012）。第三种LOV蛋白，金黄色色素（aureochrome， AUREO），在层菌藻——冷冻水蛭（Vaucheria frigida）中被鉴定出来（Takahashi et al. 2007）。AUREO具有一个基本区域/亮氨酸拉链（bZIP）结构域和一个LOV结构域，被认为是一个bl调节的转录因子。因此，植物中的LOV BL受体家族有不同的成员，这些成员在LOV结构域中由FMN的光化学反应触发多种生理功能。
Plants utilize light not only as an energy source for photosynthesis, but also as an environmental cue to direct numerous developmental and physiological processes. For this purpose, plants have evolved two main types of photoreceptors: the phytochromes (Franklin and Quail 2010), which sense red/far-red light, and the ultraviolet (UV)-A/blue light (BL)-sensing photoreceptors, which include cryptochrome (Liu et al. 2011), phototropin (Christie 2007) and other BL receptors described below. In addition, a third class of UV-B receptor, UVR8, was recently identified (Rizzini et al. 2011). The long history of research on BL receptors dates back to the initial observation made by the famous Charles Darwin, in which he found that plants were able to move towards light (Darwin and Darwin 1881). For a long time, the nature of the chromophore in BL receptors was much disputed as to whether it was a flavin or a carotenoid (Senger 1980). This issue was partially resolved through the identification of the first BL receptor, which corresponded to a flavin protein named cryptochrome (Ahmad and Cashmore 1993). Shortly after this discovery, the Briggs group demonstrated that the disrupted gene in Arabidopsis non-phototropic hypocotyl 1 (nph1) mutants encoded a BL receptor required for phototropic response (Huala et al. 1997, Christie et al. 1998). A homolog of NPH1, NON-PHOTOTROPIC HYPOCOTYL-LIKE 1 (NPL1), was soon identified (Kagawa et al. 2001); thereafter, NPH1 and NPL1 were renamed phototropin 1 (phot1) and phot2, respectively. Phototropins mediate diverse plant responses, such as chloroplast relocation movements (Kagawa et al. 2001, Sakai et al. 2001), stomatal opening (Kinoshita et al. 2001), early hypocotyl growth inhibition (Folta and Spaulding 2001), leaf flattening (Sakamoto and Briggs 2002), leaf positioning (Inoue et al. 2005), nuclear positioning (Iwabuchi et al. 2007, Tsuboi et al. 2007), sun tracking (Inoue et al. 2008b) and leaf photomorphogenesis (Kozuka et al. 2011), in which phot1 acts over a broad range of light intensities, whereas phot2 acts as a high-light sensor. These physiological responses contribute towards enhancing photosynthesis in the plant by increasing the absorption of light and CO2 (Takemiya et al. 2005). In addition to the two phototropins, a BL receptor family of proteins characteristically containing one light, oxygen or voltage (LOV) domain, an F-box and a Kelch repeat has been identified in Arabidopsis. These proteins include ZEITLUPE (ZTL), FLAVIN-BINDING KELCH REPEAT F-BOX 1 (FKF1) and LOV KELCH PROTEIN 2 (LKP2), and are proposed to regulate the circadian clock and photoperiodic flowering by controlling BL-dependent protein degradation (Ito et al. 2012). A third type of LOV protein, aureochrome (AUREO), was identified in the stramenopile alga, Vaucheria frigida (Takahashi et al. 2007). AUREO has a basic region/leucine zipper (bZIP) domain as well as a LOV domain, and is thought to act as a BL-regulated transcription factor. Thus, the LOV BL receptor family in plants has divergent members who have a variety of physiological functions triggered by the photochemical reactions of FMN in the LOV domain.