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Peer-reviewedCC BY 4.0Proceedings of the National Academy of Sciences

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

  • Heekyung Ahn1,2
  • Guanghao Guo2
  • Jan Sklenář2
  • Shania Pin Yin Keh2
  • Sung Un Huh3,2
  • Michelle T. Hulin4,2
  • Hayden Burdett1
  • Maria Sindalovskaya5,2
  • Seungjin Na6,7
  • Jihyeon Choi2
  • Nitika Mukhi5
  • He Zhao2
6 more authors
  • Lena S. Knorr2
  • Eunok Paek8
  • Mark James Banfield5
  • Frank L.H. Menke2
  • Wenbo Ma2
  • Jonathan D. G. Jones2
8 affiliations
  1. 1School of Biological Sciences, School of Biological Sciences, Institute of Molecular Plant Sciences, University of Edinburgh
  2. 2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park
  3. 3Department of Biological Science, Kunsan National University
  4. 4Department of Plant Soil and Microbial Sciences, Michigan State University
  5. 5Department of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park
  6. 6Center for Target-to-Therapeutics Research, Korea Basic Science Institute
  7. 7Convergent Analytical Science, University of Science and Technology
  8. 8Department of Computer Science, Hanyang University
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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.

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Cite

BibTeXRIS
BibTeX
@article{ahn2026recognitiondependent,
  title = {{Recognition-dependent activation of the Arabidopsis RRS1-R/RPS4 TIR-NLR immune receptor pair}},
  author = {Heekyung Ahn and Guanghao Guo and Jan Sklenář and Shania Pin Yin Keh and Sung Un Huh and Michelle T. Hulin and Hayden Burdett and Maria Sindalovskaya and Seungjin Na and Jihyeon Choi and Nitika Mukhi and He Zhao and Lena S. Knorr and Eunok Paek and Mark James Banfield and Frank L.H. Menke and Wenbo Ma and Jonathan D. G. Jones},
  journal = {Proceedings of the National Academy of Sciences},
  year = {2026},
  month = oct,
  doi = {10.1073/pnas.2611802123},
  url = {https://doi.org/10.1073/pnas.2611802123},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Recognition-dependent activation of the Arabidopsis RRS1-R/RPS4 TIR-NLR immune receptor pair
AU  - Heekyung Ahn
AU  - Guanghao Guo
AU  - Jan Sklenář
AU  - Shania Pin Yin Keh
AU  - Sung Un Huh
AU  - Michelle T. Hulin
AU  - Hayden Burdett
AU  - Maria Sindalovskaya
AU  - Seungjin Na
AU  - Jihyeon Choi
AU  - Nitika Mukhi
AU  - He Zhao
AU  - Lena S. Knorr
AU  - Eunok Paek
AU  - Mark James Banfield
AU  - Frank L.H. Menke
AU  - Wenbo Ma
AU  - Jonathan D. G. Jones
PY  - 2026
DA  - 2026/10/27
JO  - Proceedings of the National Academy of Sciences
DO  - 10.1073/pnas.2611802123
UR  - https://doi.org/10.1073/pnas.2611802123
AB  - 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.
SN  - 0027-8424
SN  - 1091-6490
ER  -