%0 Journal Article %T Structural and Functional Insights into an <i>Arabidopsis</i> NBS-LRR Receptor in <i>Nicotiana benthamiana</i> %A Jianzhong Huang %A Xiuying Guan %A Xiaoju Zhong %A Peng Jia %A Hongbin Zhang %A Honglei Ruan %J American Journal of Molecular Biology %P 84-96 %@ 2161-6663 %D 2024 %I Scientific Research Publishing %R 10.4236/ajmb.2024.142007 %X 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 <i>Arabidopsis</i>, however, its role in planta is still unclear. This study employed <i>Nicotiana benthamiana</i>, 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. %K CC-NBS-LRR %K Hypersensitive Response %K < %K i> %K Nicotiana benthamiana< %K /i> %K Plasma Membrane Localization %U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=132508