A nucleoporin is required for induction of Ca2+ spiking in legume nodule development and essential for rhizobial and fungal symbiosis
A nucleoporin is required for induction of Ca2+ spiking in legume nodule development and essential for rhizobial and fungal symbiosis
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DOI：
10.1073/pnas.0508883103
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发表时间：
2006-01-10
影响因子：
11.1
通讯作者：
Stougaard, J
中科院分区：
文献类型：
--
作者：
Kanamori, N;Madsen, LH;Stougaard, J
核-细胞质分配和细胞质与核区室之间的交通是真核细胞的基本过程。核孔复合物介导蛋白质、rna和核糖核蛋白颗粒进出细胞核的转运。在这里，我们提出了植物核孔蛋白基因Nup133的定位克隆，这是根瘤菌和菌根真菌共享的共生信号转导途径所必需的。Nup133的突变导致温度敏感的结瘤缺陷表型和菌根定植缺失。在允许的温度下，根瘤的生长频率降低是无效的，电子显微镜显示根瘤菌没有从感染线中释放出来。使用钙敏感染料测量离子通量表明，在将纯化的根瘤菌节点因子信号分子应用于根毛后几分钟内通常可检测到的Ca2+峰值需要Nup133。NUP133定位于根细胞和根毛细胞的核膜，黄色荧光蛋白融合蛋白增强，表明NUP133核孔蛋白在宿主-植物识别共生微生物后，在核-胞质快速通信中发挥了新的作用。我们的研究结果确定了一个有趣的信号过程的组成部分，该信号过程需要在细胞质膜、细胞核和质体细胞器膜上相互作用以诱导第二信使。
Nuclear-cytoplasmic partitioning and traffic between cytoplasmic and nuclear compartments are fundamental processes in eukaryotic cells. Nuclear pore complexes mediate transport of proteins, RNAs and ribonucleoprotein particles in and out of the nucleus. Here we present positional cloning of a plant nucleoporin gene, Nup133, essential for a symbiotic signal transduction pathway shared by Rhizobium bacteria and mycorrhizal fungi. Mutation of Nup133 results in a temperature sensitive nodulation deficient phenotype and absence of mycorrhizal colonization. Root nodules developing with reduced frequency at permissive temperatures are ineffective and electron microscopy show that Rhizobium bacteria are not released from infection threads. Measurement of ion fluxes using a calcium-sensitive dye show that Nup133 is required for the Ca2+ spiking normally detectable within minutes after application of purified rhizobial Nod-factor signal molecules to root hairs. Localization of NUP133 in the nuclear envelope of root cells and root hair cells shown with enhanced yellow fluorescent protein fusion proteins suggests a novel role for NUP133 nucleoporins in a rapid nuclear-cytoplasmic communication after host-plant recognition of symbiotic microbes. Our results identify a component of an intriguing signal process requiring interaction at the cell plasma membrane and at intracellular nuclear and plastid organelle-membranes to induce a second messenger.