A plant immune receptor detects pathogen effectors that target WRKY transcription factors

Panagiotis F. Sarris, Zane Duxbury, Sung Un Huh, Yan Ma, Cécile Segonzac, Jan Sklenar, Paul Derbyshire, Volkan Cevik, Ghanasyam Rallapalli, Simon B. Saucet, Lennart Wirthmueller, Frank L. H. Menke, Kee Hoon Sohn, Jonathan D. G. Jones

Research output: Contribution to journalArticlepeer-review

386 Citations (Scopus)


Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.

Original languageEnglish
Pages (from-to)1089-1100
Number of pages12
Issue number5
Publication statusPublished - 21 May 2015


  • Amino Acid Sequence
  • Arabidopsis
  • Arabidopsis Proteins
  • Bacterial Proteins
  • Innate Immunity
  • Molecular Sequence Data
  • Plant Proteins
  • Tertiary Protein Structure
  • Pseudomonas fluorescens
  • Pseudomonas syringae
  • Tobacco

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