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The potato resistance protein Rx1 multimerizes upon activation by the Coat Protein of PVX

Marijn Knip, Emy Latul, View ORCID ProfileFrank LW Takken
doi: https://doi.org/10.1101/2023.01.10.523371
Marijn Knip
University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098XH Amsterdam, The Netherlands
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Emy Latul
University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098XH Amsterdam, The Netherlands
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Frank LW Takken
University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098XH Amsterdam, The Netherlands
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  • ORCID record for Frank LW Takken
  • For correspondence: f.l.w.takken@uva.nl
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Abstract

Nucleotide-binding Leucine Rich repeat-type immune receptors (NLRs) are intracellular proteins that sense the presence of pathogen-derived elicitors and subsequently trigger an immune response. NLR proteins have to be strictly regulated as immune responses typically result in death of affected host cells. Regulation mechanisms of NLR activation are well studied, however steps immediately following NLR activation are largely unexplained. Multimerization of NLRs is thought to be involved, although currently no unambiguous paradigm regarding the dynamics of this process exists. Some NLRs form high-molecular weight complexes before activation, others exclusively after activation, or, like Rx1, none could be detected. We investigated NLR complex formation in transgenic N. benthamiana stably expressing the potato Rx1 protein from its native promoter. Activation of the Rx1-resistance response was synchronized by dexamethasone-controlled expression of its elicitor; the Potato Virus X Coat Protein. Rx1 self-associates upon activation: Rx1 homomers are absent before dexamethasone application, a complex could be detected 1 hour after application, but surprisingly is again absent after 2 hours or later. These results show that self-association of NLR proteins upon activation can be transient, explaining the difficulties of detecting them during the normal, non-synchronized infection process as this typically involves few affected cells at any time.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
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-NC-ND 4.0 International license.
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Posted January 10, 2023.
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The potato resistance protein Rx1 multimerizes upon activation by the Coat Protein of PVX
Marijn Knip, Emy Latul, Frank LW Takken
bioRxiv 2023.01.10.523371; doi: https://doi.org/10.1101/2023.01.10.523371
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The potato resistance protein Rx1 multimerizes upon activation by the Coat Protein of PVX
Marijn Knip, Emy Latul, Frank LW Takken
bioRxiv 2023.01.10.523371; doi: https://doi.org/10.1101/2023.01.10.523371

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