A method for functional testing constitutive and ligand-induced interactions of lysin motif receptor proteins
A method for functional testing constitutive and ligand-induced interactions of lysin motif receptor proteins
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一种功能测试溶素基序受体蛋白的组成型和配体诱导的相互作用的方法
DOI：
10.1186/s13007-020-0551-4
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发表时间：
2020-01-16
期刊：
影响因子：
5.1
通讯作者：
Staehelin, Christian
中科院分区：
文献类型：
--
作者：
Li, Chun-Lian;Xue, De-Xing;Staehelin, Christian
背景具有溶素基序（LsyM）的植物受体识别微生物信号，例如固氮根瘤菌的真菌几丁质和脂壳寡糖Nod因子。通常认为配体诱导的 LysM 受体二聚化是细胞内激酶结构域和下游信号传导激活的重要步骤。因此，表达植物防御和建立共生所需的基因。我们最近发现拟南芥的三种LysM受体蛋白（即LYK1、LYK4和LYK5）形成三联受体复合物来感知几丁质。然而，LysM 受体的组成型和配体诱导的相互作用通常仍然难以表征。结果使用豆科植物莲花的毛状根，通过嵌合受体方法研究了 LYK1、LYK4 和 LYK5 胞外域之间的相互作用。由 LYK 胞外域和 aL 胞内域组成的合成受体对。测试了日本刺参Nod因子受体（分别为NFR1和NFR5）激活共生NIN（结节起始）基因表达的能力。结果表明所检测的胞外域存在组成型（LYK4ED–LYK4ED、LYK4ED–LYK5ED）和几丁质诱导的相互作用（LYK1ED–LYK1ED、LYK1ED–LYK5ED）。结论我们提出了一种对 LysM 型蛋白的组成型和配体诱导的相互作用进行功能分析的方法。
BackgroundPlant receptors with lysin motifs (LsyM) recognize microbial signals such as fungal chitin and lipo-chitooligosaccharidic Nod factors of nitrogen-fixing rhizobia. It is generally assumed that ligand-induced dimerization of LysM receptors is an essential step in activation of intracellular kinase domains and downstream signaling. Consequently, genes required for plant defense and establishment of symbiosis are expressed. We recently found that three LysM receptor proteins (namely LYK1, LYK4 and LYK5) ofArabidopsis thalianaform a tripartite receptor complex to perceive chitin. However, constitutive and ligand-induced interactions of LysM receptors generally remain difficult to be characterized.ResultsInteractions between ectodomains of LYK1, LYK4 and LYK5 were investigated by a chimeric receptor approach using hairy roots of the legumeLotus japonicus. Synthetic receptor pairs consisting of a LYK ectodomain and the intracellular domain of aL. japonicusNod factor receptor (NFR1 and NFR5, respectively) were tested for their capacity to activate expression of the symbioticNIN(nodule inception) gene. The results indicated constitutive (LYK4ED–LYK4ED, LYK4ED–LYK5ED) and chitin-induced interactions (LYK1ED–LYK1ED, LYK1ED–LYK5ED) of the examined ectodomains.ConclusionWe present a method to functionally analyze constitutive and ligand-induced interactions of LysM-type proteins.