Arbuscular Mycorrhizal Symbiosis Requires a Phosphate Transceptor in the Gigaspora margarita Fungal Symbiont.
Arbuscular Mycorrhizal Symbiosis Requires a Phosphate Transceptor in the Gigaspora margarita Fungal Symbiont.
复制标题
DOI：
10.1016/j.molp.2016.08.011
复制
发表时间：
2016-12
期刊：
影响因子：
27.5
通讯作者：
Xianan Xie;Hui-Rung Lin;Xiaowei Peng;Congrui Xu;Zhongfeng Sun;Kexin Jiang;Antian Huang;Xiaohui Wu;Nianwu Tang;A. Salvioli;P. Bonfante;Bin Zhao
中科院分区：
文献类型：
--
作者：
Xianan Xie;Hui-Rung Lin;Xiaowei Peng;Congrui Xu;Zhongfeng Sun;Kexin Jiang;Antian Huang;Xiaohui Wu;Nianwu Tang;A. Salvioli;P. Bonfante;Bin Zhao
大多数陆生维管植物能够与球囊菌门的专性生物营养型丛枝菌根真菌（AM）形成互惠共生关系。这种互惠共生为真菌提供碳水化合物，而碳水化合物提高了植物对磷酸盐的吸收。AM真菌转运蛋白可以通过菌丝网络从土壤中获取磷。然而，AM真菌磷酸盐转运蛋白在真菌信号转导中的确切功能，以及它们是否作为传感器或营养转运蛋白仍不清楚。在这里，我们报告了一个高亲和力的磷酸盐转运GigmPT从Gigaspora margaritathat是所需的AM共生。在AM共生过程中，寄主诱导的GigmPTham基因沉默阻碍了珍珠棉的发育。最重要的是，GigmPT在玛格丽特酵母中作为磷酸盐转运体发挥作用，从而激活磷酸盐信号通路以及蛋白激酶A信号级联。使用取代的半胱氨酸可及性方法，我们确定了GigmPT的残基A146（跨膜结构域[TMD] IV）和Val357（TMD VIII），这两个残基对酵母生长诱导过程中的磷酸信号传导和转运至关重要。总的来说，我们的研究结果提供了显着的见解从AM真菌G.玛格丽塔磷酸盐转运蛋白的分子功能。
The majority of terrestrial vascular plants are capable of forming mutualistic associations with obligate biotrophic arbuscular mycorrhizal (AM) fungi from the phylum Glomeromycota. This mutualistic symbiosis provides carbohydrates to the fungus, and reciprocally improves plant phosphate uptake. AM fungal transporters can acquire phosphate from the soil through the hyphal networks. Nevertheless, the precise functions of AM fungal phosphate transporters, and whether they act as sensors or as nutrient transporters, in fungal signal transduction remain unclear. Here, we report a high-affinity phosphate transporter GigmPT fromGigaspora margaritathat is required for AM symbiosis. Host-induced gene silencing ofGigmPThampers the development ofG. margaritaduring AM symbiosis. Most importantly, GigmPT functions as a phosphate transceptor inG. margaritaregarding the activation of the phosphate signaling pathway as well as the protein kinase A signaling cascade. Using the substituted-cysteine accessibility method, we identified residues A146(in transmembrane domain [TMD] IV) and Val357(in TMD VIII) of GigmPT, both of which are critical for phosphate signaling and transport in yeast during growth induction. Collectively, our results provide significant insights into the molecular functions of a phosphate transceptor from the AM fungusG. margarita.