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Structure paper

TitleStructural basis of NPR1 in activating plant immunity.
Journal, issue, pagesNature, Vol. 605, Issue 7910, Page 561-566, Year 2022
Publish dateMay 11, 2022
AuthorsShivesh 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 / Pei Zhou /
PubMed AbstractNPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid. Despite the important role of NPR1 in plant immunity, understanding of its regulatory ...NPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid. Despite the important role of NPR1 in plant immunity, 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 TGA3-NPR1-TGA3 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.
External linksNature / PubMed:35545668 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 3.9 Å
Structure data

23884

7mk2

EMDB-23884, PDB-7mk2:
CryoEM Structure of NPR1
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-23885:
CryoEM Map of the NPR1-SA complex
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-25768: Cryo-EM maps of the (TGA3)2-(NPR1)2-(TGA3)2 complex
Method: EM (single particle) / Resolution: 3.6 Å

25769

7tac

EMDB-25769, PDB-7tac:
Cryo-EM structure of the (TGA3)2-(NPR1)2-(TGA3)2 complex
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-25770: cryo-EM maps of the (NPR1)2-(TGA3)2 complex
Method: EM (single particle) / Resolution: 3.6 Å

25771

7tad

EMDB-25771, PDB-7tad:
CryoEM structure of the (NPR1)2-(TGA3)2 complex
Method: EM (single particle) / Resolution: 3.6 Å

PDB-7mk3:
Crystal structure of NPR1
Method: X-RAY DIFFRACTION / Resolution: 3.06 Å

PDB-7tae:
Crystal Structure of the NPR1-Interacting Domain of TGA3
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-CL:
Unknown entry / Chloride

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-HOH:
WATER / Water

Source
  • arabidopsis thaliana (thale cress)
KeywordsPLANT PROTEIN / IMMUNE SYSTEM / NPR1 / SAR / plant immunity / TGA3 / Plant Immunity Complex / DNA BINDING PROTEIN / NPR1-interacting domain / transcription factor

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