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TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
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TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
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Journal Article
TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
2019
Overview
Nucleotide-binding leucine-rich repeat (NLR) immune receptors play a critical role in defence against pathogens in plants and animals. However, we know very little about NLR-interacting proteins and the mechanisms that regulate NLR levels. Here, we used proximity labeling (PL) to identify the proteome proximal to N, which is an NLR that confers resistance to
Tobacco mosaic virus
(TMV). Evaluation of different PL methods indicated that TurboID-based PL provides more efficient levels of biotinylation than BioID and BioID2 in plants. TurboID-based PL of N followed by quantitative proteomic analysis and genetic screening revealed multiple regulators of
N
-mediated immunity. Interestingly, a putative E3 ubiquitin ligase, UBR7, directly interacts with the TIR domain of N. UBR7 downregulation leads to an increased amount of N protein and enhanced TMV resistance. TMV-p50 effector disrupts the N-UBR7 interaction and relieves negative regulation of N. These findings demonstrate the utility of TurboID-based PL in plants and the N-interacting proteins we identified enhance our understanding of the mechanisms underlying NLR regulation.
Plant NLR receptors trigger immune signaling following recognition of pathogen effectors. Here, Zhang
et al
. optimize a TurboID-based proximity labeling approach and show that it can be used to identify interacting partners of N, an NLR that confers resistance to
Tobacco mosaic virus
.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 82/1
/ Enzymes
/ Humanities and Social Sciences
/ Immunity
/ Labeling
/ Leucine
/ Proteins
/ Receptors, Immunologic - immunology
/ Receptors, Immunologic - metabolism
/ Science
/ Signal Transduction - immunology
/ Staining and Labeling - methods
/ Tobacco
/ Tobacco Mosaic Virus - immunology
/ Tobacco Mosaic Virus - metabolism
/ Ubiquitin-Protein Ligases - immunology
/ Ubiquitin-Protein Ligases - metabolism
/ Viruses
