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Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1

Michael J. Skelly, James J. Furniss, Heather L. Grey, Ka-Wing Wong, View ORCID ProfileSteven H. Spoel
doi: https://doi.org/10.1101/582296
Michael J. Skelly
1Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK
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James J. Furniss
1Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK
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Heather L. Grey
1Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK
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Ka-Wing Wong
1Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK
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Steven H. Spoel
1Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK
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  • ORCID record for Steven H. Spoel
  • For correspondence: steven.spoel@ed.ac.uk
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ABSTRACT

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 processive 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.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted March 20, 2019.
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Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1
Michael J. Skelly, James J. Furniss, Heather L. Grey, Ka-Wing Wong, Steven H. Spoel
bioRxiv 582296; doi: https://doi.org/10.1101/582296
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Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1
Michael J. Skelly, James J. Furniss, Heather L. Grey, Ka-Wing Wong, Steven H. Spoel
bioRxiv 582296; doi: https://doi.org/10.1101/582296

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