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Plant J., Jan 25 2024, | https://doi.org/10.1111/tpj.16639 Molecular basis for the interference of the Arabidopsis WRKY54-mediated immune response by two sequence-unrelated bacterial effectors

Haseong Kim¹, Jieun Kim^1,2, Du Seok Choi^3,†, Min-Sung Kim³, Laurent Deslandes⁴, Jay Jayaraman^5,*and Kee Hoon Sohn^1,2,6,7,*

¹Plant Immunity Research Center, Seoul National University, Seoul 08826, Republic of Korea,

²Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea,

³Department of Life Sciences, Pohang University of Science and Technology, Pohang 37673, Republic of Korea,

⁴Laboratoire des Interactions Plantes-Microbes-Environnement, Universite de Toulouse, INRAE, CNRS, Castanet-Tolosan31326, France,

⁵The New Zealand Institute for Plant and Food Research Limited, Mt. Albert Research Centre, Auckland 1025, New Zealand,

⁶Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea,

⁷Plant Genomics and Breeding Institute, Seoul National University, Seoul 08826, Republic of Korea

^*For correspondence : Jay Jayaraman and Kee Hoon Sohn

^†Present address: LG Chem, LG Science Park, Seoul 07796, Republic of Korea

Abstract

Arabidopsis thaliana WRKY proteins are potential targets of pathogen-secreted effectors. RESISTANT TO RALSTONIA SOLANACEARUM 1 (RRS1; AtWRKY52) is a well-studied Arabidopsis nucleotide-binding and leucine-rich repeat (NLR) immune receptor carrying a C-terminal WRKY domain that functions as an integrated decoy. RRS1-R recognizes the effectors AvrRps4 from Pseudomonas syringae pv. pisi and PopP2 from Ralstonia pseudosolanacearum by direct interaction through its WRKY domain. AvrRps4 and PopP2 were previously shown to interact with several AtWRKYs. However, how these effectors selectively interact with their virulence targets remains unknown. Here, we show that several members of subgroup IIIb of the AtWRKY family are targeted by AvrRps4 and PopP2. We demonstrate that several AtWRKYs induce cell death when transiently expressed in Nicotiana benthamiana, indicating the activation of immune responses. AtWRKY54 was the only cell death-inducing AtWRKY that interacted with both AvrRps4 and PopP2. We found that AvrRps4 and PopP2 specifically suppress AtWRKY54-induced cell death. We also demonstrate that the amino acid residues required for the avirulence function of AvrRps4 and PopP2 are critical for suppressing AtWRKY54-induced cell death. AtWRKY54 residues predicted to form a binding interface with AvrRps4 were predominantly located in the DNA binding domain and necessary for inducing cell death. Notably, one AtWRKY54 residue, E164, contributes to affinity with AvrRps4 and is exclusively present among subgroup IIIb AtWRKYs, yet is located outside of the DNA-binding domain. Surprisingly, AtWRKY54 mutated at E164 evaded AvrRps4-mediated cell death suppression. Taking our observations together, we propose that AvrRp4 and PopP2 specifically target AtWRKY54 to suppress plant immune responses.

논문정보

형식Research article
게재일2024년 01월 (BRIC 등록일 2024-01-26)
연구진국내(교신)+국외 연구진
분야 생명과학 > 식물학

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