Recognition-dependent activation of the Arabidopsis RRS1-R/RPS4 TIR-NLR immune receptor pair

Plant TIR domain-containing proteins exhibit NADase activity upon pathogen effector recognition, creating small molecules that activate defense via EDS1 and its associated proteins. Arabidopsis RPS4 and RRS1 comprise a TIR-NLR immune receptor pair that recognizes multiple effector proteins including AvrRps4 and PopP2. We show here that RPS4 and RRS1 acquire NADase activity upon recognition of a cognate effector. However, both in the presence and absence of effector, RPS4 and RRS1 form an oligomer that does not change in size upon effector provision. Effector-dependent defense activation by RPS4 and RRS1 requires the catalytic glutamate residue and the BB-loop motif of RPS4, which is absent in RRS1 and other RRS1-like TIR domains in Arabidopsis . Oligomerization of RPS4 and RRS1 occurs through multiple domains, but oligomerization does not require enzymatic activity. We propose that conformational changes or reconfiguration within the RPS4/RRS1 oligomer upon effector recognition derepresses the complex for immune activation.

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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2026-10-27
DOI
https://doi.org/10.1073/pnas.2611802123
Primary Topic
Plant-Microbe Interactions and Immunity
Type
article
Field-Weighted Citation Impact
0.00

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article

Recognition-dependent activation of the Arabidopsis RRS1-R/RPS4 TIR-NLR immune receptor pair

Jonathan D. G. Jones, Frank L.H. Menke, Sung Un Huh, Michelle T. Hulin et al.
Proceedings of the National Academy of Sciences
Plant-Microbe Interactions and Immunity
article

Recognition-dependent activation of the Arabidopsis RRS1-R/RPS4 TIR-NLR immune receptor pair

Jonathan D. G. Jones, Frank L.H. Menke, Sung Un Huh, Michelle T. Hulin, Maria Sindalovskaya, Guanghao Guo, Hayden Burdett, Jihyeon Choi, Mark James Banfield, Jan Sklenář, Wenbo Ma, Nitika Mukhi, Eunok Paek, Seungjin Na, He Zhao, Heekyung Ahn, Shania Pin Yin Keh, Lena Knorr
article en

Abstract

Plant TIR domain-containing proteins exhibit NADase activity upon pathogen effector recognition, creating small molecules that activate defense via EDS1 and its associated proteins. Arabidopsis RPS4 and RRS1 comprise a TIR-NLR immune receptor pair that recognizes multiple effector proteins including AvrRps4 and PopP2. We show here that RPS4 and RRS1 acquire NADase activity upon recognition of a cognate effector. However, both in the presence and absence of effector, RPS4 and RRS1 form an oligomer that does not change in size upon effector provision. Effector-dependent defense activation by RPS4 and RRS1 requires the catalytic glutamate residue and the BB-loop motif of RPS4, which is absent in RRS1 and other RRS1-like TIR domains in Arabidopsis . Oligomerization of RPS4 and RRS1 occurs through multiple domains, but oligomerization does not require enzymatic activity. We propose that conformational changes or reconfiguration within the RPS4/RRS1 oligomer upon effector recognition derepresses the complex for immune activation.

Proceedings of the National Academy of SciencesVol. 123(44)
John Innes Centre (GB), University of East Anglia (GB), Kunsan National University (KR), Norwich Research Park (GB), Sainsbury Laboratory (GB), Convergent Science (United States) (US), Korea Basic Science Institute (KR), Hanyang University (KR), Michigan State University (US), University of Edinburgh (GB)
Royal Society, Gatsby Charitable Foundation, Korea Basic Science Institute, Biotechnology and Biological Sciences Research Council, Institute for Information and Communications Technology Promotion, HORIZON EUROPE European Research Council
Openalex Percentile: Top 15%
Plant-Microbe Interactions and Immunity
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