Structural basis of NPR1 in activating plant immunity

Shivesh Kumar, Raul Zavaliev, Qinglin Wu, Ye Zhou, Jie Cheng, Lucas Dillard, Jordan Powers, John Withers, Jinshi Zhao, Ziqiang Guan, Mario J. Borgnia, Alberto Bartesaghi, Xinnian Dong () and Pei Zhou ()
Additional contact information
Shivesh Kumar: Duke University School of Medicine
Raul Zavaliev: Duke University
Qinglin Wu: Duke University School of Medicine
Ye Zhou: Duke University
Jie Cheng: Duke University School of Medicine
Lucas Dillard: National Institute of Environmental Health Sciences, NIH, Department of Health and Human Services
Jordan Powers: Duke University
John Withers: Duke University
Jinshi Zhao: Duke University School of Medicine
Ziqiang Guan: Duke University School of Medicine
Mario J. Borgnia: National Institute of Environmental Health Sciences, NIH, Department of Health and Human Services
Alberto Bartesaghi: Duke University School of Medicine
Xinnian Dong: Duke University
Pei Zhou: Duke University School of Medicine

Nature, 2022, vol. 605, issue 7910, 561-566

Abstract: Abstract NPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid1–4. Despite the important role of NPR1 in plant immunity5–7, understanding of its regulatory mechanisms has been hindered by a lack of structural information. Here we report cryo-electron microscopy and crystal structures of Arabidopsis NPR1 and its complex with the transcription factor TGA3. Cryo-electron microscopy analysis reveals that NPR1 is a bird-shaped homodimer comprising a central Broad-complex, Tramtrack and Bric-à-brac (BTB) domain, a BTB and carboxyterminal Kelch helix bundle, four ankyrin repeats and a disordered salicylic-acid-binding domain. Crystal structure analysis reveals a unique zinc-finger motif in BTB for interacting with ankyrin repeats and mediating NPR1 oligomerization. We found that, after stimulation, salicylic-acid-induced folding and docking of the salicylic-acid-binding domain onto ankyrin repeats is required for the transcriptional cofactor activity of NPR1, providing a structural explanation for a direct role of salicylic acid in regulating NPR1-dependent gene expression. Moreover, our structure of the TGA32–NPR12–TGA32 complex, DNA-binding assay and genetic data show that dimeric NPR1 activates transcription by bridging two fatty-acid-bound TGA3 dimers to form an enhanceosome. The stepwise assembly of the NPR1–TGA complex suggests possible hetero-oligomeric complex formation with other transcription factors, revealing how NPR1 reprograms the defence transcriptome.

Date: 2022
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DOI: 10.1038/s41586-022-04699-w

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