Kim Nak Hyun, Hwang Byung Kook
Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-713, Republic of Korea.
Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-713, Republic of Korea
Plant Physiol. 2015 Feb;167(2):307-22. doi: 10.1104/pp.114.253898. Epub 2014 Dec 9.
Heat shock proteins (HSPs) function as molecular chaperones and are essential for the maintenance and/or restoration of protein homeostasis. The genus Xanthomonas type III effector protein AvrBsT induces hypersensitive cell death in pepper (Capsicum annuum). Here, we report the identification of the pepper CaHSP70a as an AvrBsT-interacting protein. Bimolecular fluorescence complementation and coimmunoprecipitation assays confirm the specific interaction between CaHSP70a and AvrBsT in planta. The CaHSP70a peptide-binding domain is essential for its interaction with AvrBsT. Heat stress (37°C) and Xanthomonas campestris pv vesicatoria (Xcv) infection distinctly induce CaHSP70a in pepper leaves. Cytoplasmic CaHSP70a proteins significantly accumulate in pepper leaves to induce the hypersensitive cell death response by Xcv (avrBsT) infection. Transient CaHSP70a overexpression induces hypersensitive cell death under heat stress, which is accompanied by strong induction of defense- and cell death-related genes. The CaHSP70a peptide-binding domain and ATPase-binding domain are required to trigger cell death under heat stress. Transient coexpression of CaHSP70a and avrBsT leads to cytoplasmic localization of the CaHSP70a-AvrBsT complex and significantly enhances avrBsT-triggered cell death in Nicotiana benthamiana. CaHSP70a silencing in pepper enhances Xcv growth but disrupts the reactive oxygen species burst and cell death response during Xcv infection. Expression of some defense marker genes is significantly reduced in CaHSP70a-silenced leaves, with lower levels of the defense hormones salicylic acid and jasmonic acid. Together, these results suggest that CaHSP70a interacts with the type III effector AvrBsT and is required for cell death and immunity in plants.
热休克蛋白(HSPs)作为分子伴侣发挥作用,对于维持和/或恢复蛋白质稳态至关重要。野油菜黄单胞菌属III型效应蛋白AvrBsT可诱导辣椒(辣椒属)中的过敏细胞死亡。在此,我们报告鉴定出辣椒CaHSP70a为一种与AvrBsT相互作用的蛋白。双分子荧光互补和免疫共沉淀分析证实了CaHSP70a与AvrBsT在植物体内的特异性相互作用。CaHSP70a肽结合结构域对其与AvrBsT的相互作用至关重要。热胁迫(37°C)和野油菜黄单胞菌辣椒斑点病致病型(Xcv)感染可显著诱导辣椒叶片中CaHSP70a的表达。细胞质CaHSP70a蛋白在辣椒叶片中大量积累,以诱导Xcv(avrBsT)感染引发的过敏细胞死亡反应。CaHSP70a的瞬时过表达在热胁迫下诱导过敏细胞死亡,同时伴随着防御和细胞死亡相关基因的强烈诱导。CaHSP70a肽结合结构域和ATP酶结合结构域是热胁迫下触发细胞死亡所必需的。CaHSP70a和avrBsT的瞬时共表达导致CaHSP70a-AvrBsT复合物定位于细胞质,并显著增强avrBsT在本氏烟草中引发的细胞死亡。辣椒中CaHSP70a的沉默增强了Xcv的生长,但破坏了Xcv感染期间的活性氧爆发和细胞死亡反应。在CaHSP70a沉默的叶片中,一些防御标记基因的表达显著降低,水杨酸和茉莉酸等防御激素的水平也较低。总之,这些结果表明CaHSP70a与III型效应蛋白AvrBsT相互作用,是植物细胞死亡和免疫所必需的。