Dissecting Multiple Arabidopsis CC-NBS-LRR Proteins Structure and Localization  

作　　者：Jianzhong Huang Xiuying Guan Xiaoju Zhong Peng Jia Hongbin Zhang Kai Chen Zhuojun Li Guangyu Chen Chuitang Zeng Jianzhong Huang;Xiuying Guan;Xiaoju Zhong;Peng Jia;Hongbin Zhang;Kai Chen;Zhuojun Li;Guangyu Chen;Chuitang Zeng(Key Research Laboratory of Chronic Disease, Fuzhou Medical University, Fuzhou, China;Technology Innovation Center of Chronic Disease Research in Fuzhou City, Fuzhou Science and Technology Bureau, Fuzhou, China)

机构地区：[1]Key Research Laboratory of Chronic Disease, Fuzhou Medical University, Fuzhou, China [2]Technology Innovation Center of Chronic Disease Research in Fuzhou City, Fuzhou Science and Technology Bureau, Fuzhou, China

出　　处：《Journal of Biosciences and Medicines》2024年第7期87-99,共13页生物科学与医学（英文）

摘　　要：NBS-LRR (nucleotide binding sites and leucine rich repeat) protein plays a crucial role as sentries and as defense activators in plants. The structure and function of NBS-LRR proteins are closely related. Previous articles have announced that the activated ZAR1 (HopZ-Activated Resistance 1) forms a pentamer in the plasma membrane, which is a calcium permeable channel that can trigger plant immune signaling and cell death. However, the structure of galore NBS-LRRs in Arabidopsis is not yet clear. The functional sites of distinct NBS-LRR in cells may vary. In addition, identifying pathogens and activating defense regions may occur in different subcellular compartments. Therefore, dissecting the specific structure and positioning of NBS-LRRs is an indispensable step in understanding their functions. In this article, we exploit AlphaFold to predict the structure of some designed NBS-LRRs, and utilize Agroinfiltration transient expression system, combined with biochemical fractionation, to dissect the localization of these NBS-LRR receptors from Arabidopsis. Structural data indicates that the identified NBS-LRRs share analogous conformation. Membrane fractionation assay demonstrates these NBS-LRRs are mainly associated with the membrane. These data show that the Ca2+-permeable channel activity may be evolutionarily conserved in NBS-LRR of Arabidopsis, and this study provides some reference clues for analyzing the structure and localization patterns of other plant immune receptors.NBS-LRR (nucleotide binding sites and leucine rich repeat) protein plays a crucial role as sentries and as defense activators in plants. The structure and function of NBS-LRR proteins are closely related. Previous articles have announced that the activated ZAR1 (HopZ-Activated Resistance 1) forms a pentamer in the plasma membrane, which is a calcium permeable channel that can trigger plant immune signaling and cell death. However, the structure of galore NBS-LRRs in Arabidopsis is not yet clear. The functional sites of distinct NBS-LRR in cells may vary. In addition, identifying pathogens and activating defense regions may occur in different subcellular compartments. Therefore, dissecting the specific structure and positioning of NBS-LRRs is an indispensable step in understanding their functions. In this article, we exploit AlphaFold to predict the structure of some designed NBS-LRRs, and utilize Agroinfiltration transient expression system, combined with biochemical fractionation, to dissect the localization of these NBS-LRR receptors from Arabidopsis. Structural data indicates that the identified NBS-LRRs share analogous conformation. Membrane fractionation assay demonstrates these NBS-LRRs are mainly associated with the membrane. These data show that the Ca2+-permeable channel activity may be evolutionarily conserved in NBS-LRR of Arabidopsis, and this study provides some reference clues for analyzing the structure and localization patterns of other plant immune receptors.

关 键 词：ARABIDOPSIS Calcium Permeation Channel PENTAMER Plasma Membrane 

分 类 号：Q94[生物学—植物学]