Asset Details
Do you wish to reserve the book?
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
Do you wish to request the book?
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
2024
Overview
Nucleotide-binding leucine-rich repeat (NLR) proteins play a pivotal role in plant immunity by recognizing pathogen effectors
1
,
2
. Maintaining a balanced immune response is crucial, as excessive NLR expression can lead to unintended autoimmunity
3
,
4
. Unlike most NLRs, the plant NLR required for cell death 2 (NRC2) belongs to a small NLR group characterized by constitutively high expression without self-activation
5
. The mechanisms underlying NRC2 autoinhibition and activation are not yet understood. Here we show that
Solanum lycopersicum
(tomato) NRC2 (
Sl
NRC2) forms dimers and tetramers and higher-order oligomers at elevated concentrations. Cryo-electron microscopy shows an inactive conformation of
Sl
NRC2 in these oligomers. Dimerization and oligomerization not only stabilize the inactive state but also sequester
Sl
NRC2 from assembling into an active form. Mutations at the dimeric or interdimeric interfaces enhance pathogen-induced cell death and immunity in
Nicotiana
benthamiana
. The cryo-electron microscopy structures unexpectedly show inositol hexakisphosphate (IP
6
) or pentakisphosphate (IP
5
) bound to the inner surface of the C-terminal leucine-rich repeat domain of
Sl
NRC2, as confirmed by mass spectrometry. Mutations at the inositol phosphate-binding site impair inositol phosphate binding of
Sl
NRC2 and pathogen-induced
Sl
NRC2-mediated cell death in
N. benthamiana
. Our study indicates a negative regulatory mechanism of NLR activation and suggests inositol phosphates as cofactors of NRCs.
Cryo-electron microscopy reveals that the tomato immune receptor NRC2 forms oligomers to stabilize its inactive state and sequester it from activation, with inositol phosphates acting as immunoregulatory cofactors.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 38/1
/ 38/39
/ 38/61
/ 82/1
/ 82/16
/ 82/29
/ 82/58
/ 82/80
/ 82/83
/ Humanities and Social Sciences
/ Leucine
/ Mutation
/ NLR Proteins - antagonists & inhibitors
/ NLR Proteins - ultrastructure
/ Plant Proteins - antagonists & inhibitors
/ Plant Proteins - ultrastructure
/ Proteins
/ Regulatory mechanisms (biology)
/ Science
/ Sensors
/ Solanum lycopersicum - cytology
/ Solanum lycopersicum - genetics
/ Solanum lycopersicum - immunology
/ Solanum lycopersicum - metabolism
/ Tomatoes
