Delaney, T. P., Friedrich, L. & Ryals, J. A. Arabidopsis signal transduction mutant defective in chemically and biologically induced disease resistance. Proc. Natl Acad. Sci. USA 92, 6602–6606 (1995).
Shah, J., Tsui, F. & Klessig, D. F. Characterization of a salicylic acid-insensitive mutant (sai1) of Arabidopsis thaliana, identified in a selective screen utilizing the SA-inducible expression of the tms2 gene. Mol. Plant Microbe Interact. 10, 69–78 (1997).
Cao, H., Bowling, S. A., Gordon, A. S. & Dong, X. Characterization of an Arabidopsis mutant that is nonresponsive to inducers of systemic acquired resistance. Plant Cell 6, 1583–1592 (1994).
Glazebrook, J., Rogers, E. E. & Ausubel, F. M. Isolation of Arabidopsis mutants with enhanced disease susceptibility by direct screening. Genetics 143, 973–982 (1996).
Ryals, J. et al. The Arabidopsis NIM1 protein shows homology to the mammalian transcription factor inhibitor I kappa B. Plant Cell 9, 425–439 (1997).
Cao, H., Glazebrook, J., Clarke, J. D., Volko, S. & Dong, X. The Arabidopsis NPR1 gene that controls systemic acquired resistance encodes a novel protein containing ankyrin repeats. Cell 88, 57–63 (1997).
Backer, R., Naidoo, S. & van den Berg, N. The NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1) and related family: mechanistic insights in plant disease resistance. Front. Plant Sci. 10, 102 (2019).
Silva, K. J. P., Mahna, N., Mou, Z. & Folta, K. M. NPR1 as a transgenic crop protection strategy in horticultural species. Hortic. Res. 5, 15 (2018).
Stogios, P. J., Downs, G. S., Jauhal, J. J., Nandra, S. K. & Prive, G. G. Sequence and structural analysis of BTB domain proteins. Genome Biol. 6, R82 (2005).
Stogios, P. J. & Prive, G. G. The BACK domain in BTB-kelch proteins. Trends Biochem. Sci. 29, 634–637 (2004).
Canning, P. et al. Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. J. Biol. Chem. 288, 7803–7814 (2013).
Zhuang, M. et al. Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Mol. Cell 36, 39–50 (2009).
Errington, W. J. et al. Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. Structure 20, 1141–1153 (2012).
Gorina, S. & Pavletich, N. P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274, 1001–1005 (1996).
Li, J., Mahajan, A. & Tsai, M. D. Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry 45, 15168–15178 (2006).
Sedgwick, S. G. & Smerdon, S. J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24, 311–316 (1999).
Wang, W. et al. Structural basis of salicylic acid perception by Arabidopsis NPR proteins. Nature 586, 311–316 (2020).
Mou, Z., Fan, W. & Dong, X. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 113, 935–944 (2003).
Canet, J. V., Dobon, A., Roig, A. & Tornero, P. Structure-function analysis of npr1 alleles in Arabidopsis reveals a role for its paralogs in the perception of salicylic acid. Plant Cell Environ. 33, 1911–1922 (2010).
Bombarda, E., Cherradi, H., Morellet, N., Roques, B. P. & Mely, Y. Zn2+ binding properties of single-point mutants of the C-terminal zinc finger of the HIV-1 nucleocapsid protein: evidence of a critical role of cysteine 49 in Zn2+ dissociation. Biochemistry 41, 4312–4320 (2002).
Hol, W. G. Effects of the alpha-helix dipole upon the functioning and structure of proteins and peptides. Adv. Biophys. 19, 133–165 (1985).
Tada, Y. et al. Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins. Science 321, 952–956 (2008).
Manohar, M. et al. Identification of multiple salicylic acid-binding proteins using two high throughput screens. Front. Plant Sci. 5, 777 (2014).
Ding, Y. et al. Opposite roles of salicylic acid receptors NPR1 and NPR3/NPR4 in transcriptional regulation of plant immunity. Cell 173, 1454–1467 (2018).
Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 46, W296–W303 (2018).
Saleh, A. et al. Posttranslational modifications of the master transcriptional regulator NPR1 enable dynamic but tight control of plant immune responses. Cell Host Microbe 18, 169–182 (2015).
Maier, F. et al. NONEXPRESSOR OF PATHOGENESIS-RELATED PROTEINS1 (NPR1) and some NPR1-related proteins are sensitive to salicylic acid. Mol. Plant Pathol. 12, 73–91 (2011).
Hermann, M. et al. The Arabidopsis NIMIN proteins affect NPR1 differentially. Front. Plant Sci. 4, 88 (2013).
Lebel, E. et al. Functional analysis of regulatory sequences controlling PR-1 gene expression in Arabidopsis. Plant J. 16, 223–233 (1998).
Kachroo, A. & Kachroo, P. Fatty acid-derived signals in plant defense. Annu. Rev. Phytopathol. 47, 153–176 (2009).
Fu, Z. Q. & Dong, X. Systemic acquired resistance: turning local infection into global defense. Annu. Rev. Plant Biol. 64, 839–863 (2013).
Wang, D., Amornsiripanitch, N. & Dong, X. A genomic approach to identify regulatory nodes in the transcriptional network of systemic acquired resistance in plants. PLoS Pathog. 2, e123 (2006).
Pape, S., Thurow, C. & Gatz, C. The Arabidopsis PR-1 promoter contains multiple integration sites for the coactivator NPR1 and the repressor SNI1. Plant Physiol. 154, 1805–1818 (2010).
Sievers, F. et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539 (2011).
Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).
Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004).
Afonine, P. V. et al. Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr. D 74, 531–544 (2018).
Bepler, T. et al. Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs. Nat. Methods 16, 1153–1160 (2019).
Kabsch, W. XDS. Acta Crystallogr. D 66, 125–132 (2010).
Bligh, E. G. & Dyer, W. J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911–917 (1959).
Li, C., Tan, B. K., Zhao, J. & Guan, Z. In vivo and in vitro synthesis of phosphatidylglycerol by an Escherichia coli cardiolipin synthase. J. Biol. Chem. 291, 25144–25153 (2016).
Spoel, S. H. et al. Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity. Cell 137, 860–872 (2009).
Zavaliev, R., Mohan, R., Chen, T. & Dong, X. Formation of NPR1 condensates promotes cell survival during the plant immune response. Cell 182, 1093–1108 (2020).
Clough, S. J. & Bent, A. F. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735–743 (1998).
Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676–682 (2012).
Zavaliev, R. & Epel, B. L. Imaging callose at plasmodesmata using aniline blue: quantitative confocal microscopy. Methods Mol. Biol. 1217, 105–119 (2015).
