Tameling, W.I.L., Vossen, J.H., Albrecht, M., Lengauer, T., Berden, J.A., Haring, M.A., Cornelissen, B.J.C. and Takken, F.L.W. (2006) Mutations in the NB-ARC Domain of I-2 that Impair ATP Hydrolysis Cause Autoactivation. Plant Physiology, 140, 1233-1245.
https://doi.org/10.1104/pp.105.073510

has been cited by the following article:

• TITLE: Structural and Functional Insights into an Arabidopsis NBS-LRR Receptor in Nicotiana benthamiana

  AUTHORS: Jianzhong Huang, Xiuying Guan, Xiaoju Zhong, Peng Jia, Hongbin Zhang, Honglei Ruan

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

  JOURNAL NAME: American Journal of Molecular Biology, Vol.14 No.2, April 18, 2024

  ABSTRACT: 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.