Dual roles for the variable domain in protein trafficking and host-specific recognition of Heterodera glycines CLE effector proteins.
Dual roles for the variable domain in protein trafficking and host-specific recognition of Heterodera glycines CLE effector proteins.
复制标题
可变结构域在蛋白质运输和大豆胞囊线虫 CLE 效应蛋白的宿主特异性识别中发挥双重作用。
作者：
Jianying Wang;Chris Lee;Amy J Replogle;Sneha Joshi;Dmitry Korkin;R. Hussey;T. Baum;E. Davis;Xiaohong Wang;M. Mitchum
*大豆包囊线虫（Heterodera glycines）分泌的效应蛋白作为植物CLAVATA3/ESR （CLE）样肽的肽模拟物，可能参与根细胞的发育重编程，形成称为合胞体的特殊进食细胞。*然而，线虫将CLE效应物传递给寄主植物细胞的作用位点和机制尚未确定。本研究采用免疫学、遗传学和生物化学等方法，揭示了H.甘氨酸分泌的CLE蛋白在植物中的定位和作用部位。*我们提供的证据表明，线虫CLE前肽被递送到合胞细胞的细胞质中，但最终在外质体中起作用，这与它们作为植物CLE肽的配体模拟物的作用一致。我们确定线虫的12个氨基酸CLE基序肽在体内不具备足够的生物活性，这表明CLE基序上游的序列在功能中起着重要作用。*遗传和生化分析证实了植物中可变结构域对宿主特异性识别的要求，并揭示了一个新的作用，即在细胞质将cle运送到外质体中，以充当配体模拟物。
*Soybean cyst nematodes (Heterodera glycines) produce secreted effector proteins that function as peptide mimics of plant CLAVATA3/ESR (CLE)-like peptides probably involved in the developmental reprogramming of root cells to form specialized feeding cells called syncytia. *The site of action and mechanism of delivery of CLE effectors to host plant cells by the nematode, however, have not been established. In this study, immunologic, genetic and biochemical approaches were used to reveal the localization and site of action of H. glycines-secreted CLE proteins in planta. *We present evidence indicating that the nematode CLE propeptides are delivered to the cytoplasm of syncytial cells, but ultimately function in the apoplast, consistent with their proposed role as ligand mimics of plant CLE peptides. We determined that the nematode 12-amino-acid CLE motif peptide is not sufficient for biological activity in vivo, pointing to an important role for sequences upstream of the CLE motif in function. *Genetic and biochemical analysis confirmed the requirement of the variable domain in planta for host-specific recognition and revealed a novel role in trafficking cytoplasmically delivered CLEs to the apoplast in order to function as ligand mimics.