Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1

Activation of systemic acquired resistance in plants is associated with transcriptome reprogramming induced by the unstable coactivator NPR1. Immune-induced ubiquitination and proteasomal degradation of NPR1 are thought to facilitate continuous delivery of active NPR1 to target promoters, thereby ma...

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Bibliographic Details
Published in:eLife 2019-10, Vol.8
Main Authors: Skelly, Michael J, Furniss, James J, Grey, Heather, Wong, Ka-Wing, Spoel, Steven H
Format: Article
Language:English
Subjects:
Arabidopsis
Arabidopsis - immunology
Arabidopsis Proteins - metabolism
Arabidopsis thaliana
Bacteria
Biochemistry
Chromatin
Crop yields
Crops, Agricultural - immunology
Cullin
Development and progression
Disease susceptibility
Experiments
Food
Food supply
Gene expression
Genes
Genetic aspects
Health aspects
Immune response
Immune system
Ligases
Medical research
Mutation
NPR1
Pathogenic microorganisms
Pathogens
Phosphorylation
Plant Biology
Plant genetics
plant immunity
Plants (Organisms)
Proteasome Endopeptidase Complex - metabolism
Proteasomes
Proteins
salicylic acid
systemic acquired resistance
Transcription
Transcription (Genetics)
Transcription, Genetic
Ubiquitin
Ubiquitin-protein ligase
Ubiquitination
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Summary:Activation of systemic acquired resistance in plants is associated with transcriptome reprogramming induced by the unstable coactivator NPR1. Immune-induced ubiquitination and proteasomal degradation of NPR1 are thought to facilitate continuous delivery of active NPR1 to target promoters, thereby maximising gene expression. Because of this potentially costly sacrificial process, we investigated if ubiquitination of NPR1 plays transcriptional roles prior to its proteasomal turnover. Here we show ubiquitination of NPR1 is a progressive event in which initial modification by a Cullin-RING E3 ligase promotes its chromatin association and expression of target genes. Only when polyubiquitination of NPR1 is enhanced by the E4 ligase, UBE4, it is targeted for proteasomal degradation. Conversely, ubiquitin ligase activities are opposed by UBP6/7, two proteasome-associated deubiquitinases that enhance NPR1 longevity. Thus, immune-induced transcriptome reprogramming requires sequential actions of E3 and E4 ligases balanced by opposing deubiquitinases that fine-tune activity of NPR1 without strict requirement for its sacrificial turnover.
ISSN:2050-084X
2050-084X
DOI:10.7554/elife.47005