%0 Journal Article
%T Dissecting Multiple Arabidopsis CC-NBS-LRR Proteins Structure and Localization
%A Jianzhong Huang
%A Xiuying Guan
%A Xiaoju Zhong
%A Peng Jia
%A Hongbin Zhang
%A Kai Chen
%A Zhuojun Li
%A Guangyu Chen
%A Chuitang Zeng
%J Journal of Biosciences and Medicines
%P 87-99
%@ 2327-509X
%D 2024
%I Scientific Research Publishing
%R 10.4236/jbm.2024.127008
%X 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.
%K Arabidopsis
%K Calcium Permeation Channel
%K Pentamer
%K Plasma Membrane
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=134508