Author(s)

Jianzhong Huang^*, Xiuying Guan, Xiaoju Zhong, Peng Jia, Hongbin Zhang, Honglei Ruan

Key Laboratory of Chronic Diseases, Fuzhou Medical University, Fuzhou, China.

Nucleotide-binding site leucine-rich repeat receptors (NBS-LRR/NLRs) are crucial intracellular immune proteins in plants. Previous article reported a novel NLR protein SUT1 (SUPPRESSORS OF TOPP4-1, 1), which is involved in autoimmunity initiated by type one protein phosphatase 4 mutation (topp4-1) in Arabidopsis, however, its role in planta is still unclear. This study employed Nicotiana benthamiana, a model platform, to conduct an overall structural and functional analysis of SUT1 protein. The transient expression results revealed that SUT1 is a typical CNL (CC-NBS-LRR) receptor, both fluorescence data and biochemical results showed the protein is mainly anchored on the plasma membrane due to its N-terminal acylation site. Further truncation experiments announced that its CC (coiled-coil) domain possessed cell-death-inducing activity. The outcomes of point mutations analysis revealed that not only the CC domain, but also the full-length SUT1 protein, whose function and subcellular localization are influenced by highly conserved hydrophobic residues. These research outcomes provided favorable clues for elucidating the activation mechanism of SUT1.

CC-NBS-LRR, Hypersensitive Response, Nicotiana benthamiana, Plasma Membrane Localization

Huang, J. , Guan, X. , Zhong, X. , Jia, P. , Zhang, H. and Ruan, H. (2024) Structural and Functional Insights into an Arabidopsis NBS-LRR Receptor in Nicotiana benthamiana. American Journal of Molecular Biology, 14, 84-96. doi: 10.4236/ajmb.2024.142007.