Balanced plant helper NLR activation by a modified host protein complex

Shijia Huang, Junli Wang, Ridan Song, Aolin Jia, Yu Xiao, Yue Sun, Lin Wang, Dennis Mahr, Zhongshou Wu, Zhifu Han, Xin Li, Jane E. Parker () and Jijie Chai ()
Additional contact information
Shijia Huang: Westlake University
Junli Wang: Max Planck Institute for Plant Breeding Research
Ridan Song: Tsinghua University
Aolin Jia: Henan Agricultural University
Yu Xiao: Tsinghua University
Yue Sun: Westlake University
Lin Wang: Westlake University
Dennis Mahr: Max Planck Institute for Plant Breeding Research
Zhongshou Wu: University of British Columbia
Zhifu Han: Westlake University
Xin Li: University of British Columbia
Jane E. Parker: Max Planck Institute for Plant Breeding Research
Jijie Chai: Westlake University

Nature, 2025, vol. 639, issue 8054, 447-455

Abstract: Abstract Nucleotide-binding leucine-rich repeat (NLR) receptors play crucial roles in plant immunity by sensing pathogen effectors1. In Arabidopsis, certain sensor NLRs function as NADases to catalyse the production of second messengers2,3, which can be recognized by enhanced disease susceptibility 1 (EDS1) with its partner senescence-associated gene 101 (SAG101), to activate helper NLR N requirement gene 1 (NRG1)4. A cryoelectron microscopy structure shows that second-messenger-activated EDS1–SAG101 mainly contacts the leucine-rich repeat domain of NRG1A to mediate the formation of an induced EDS1–SAG101–NRG1A complex. Structural comparisons show that binding of a second messenger induces conformational changes in EDS1–SAG101, which are recognized by NRG1A, leading to its allosteric activation. We further show that an inhibitory NRG1 family member, NRG1C, efficiently outcompetes NRG1A for binding to second-messenger-activated EDS1–SAG101. These findings uncover mechanisms for NRG1A activation through its recognition of a modified host EDS1–SAG101 complex, and NRG1A inhibition by NRG1C through sequestration of the activated EDS1–SAG101, thus shedding light on the activation and constraint of a central plant immune response system.

Date: 2025
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41586-024-08521-7 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:639:y:2025:i:8054:d:10.1038_s41586-024-08521-7

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-024-08521-7

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().