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Bernoux, M., Ve, T., Williams, S., Warren, C., Hatters, D., Valkov, E., Zhang, X., Ellis, J., Kobe, B. and Dodds, P. (2011) Structural and Functional Analysis of a Plant Resistance Protein TIR Domain Reveals Interfaces for Self-Association, Signaling, and Autoregulation. Cell Host & Microbe, 9, 200-211.
https://doi.org/10.1016/j.chom.2011.02.009

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.