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Plant nucleotide-binding leucine-rich repeat (NB-LRR) disease resistance (R) proteins recognize specific “avirulent” pathogen effectors and activate immune responses. NB-LRR proteins structurally and functionally resemble mammalian Nod-like receptors (NLRs). How NB-LRR and NLR proteins activate defense is poorly understood. The divergently transcribed Arabidopsis  R  genes,  RPS4  (resistance to  Pseudomonas syringae  4) and  RRS1  (resistance to  Ralstonia solanacearum  1), function together to confer recognition of  Pseudomonas  AvrRps4 and  Ralstonia  PopP2.  RRS1  is the only known recessive NB-LRR  R  gene and encodes a WRKY DNA binding domain, prompting suggestions that it acts downstream of RPS4 for transcriptional activation of defense genes. We define here the early RRS1-dependent transcriptional changes upon delivery of PopP2  via Pseudomonas  type III secretion. The Arabidopsis  slh1  ( sensitive to low humidity 1 ) mutant encodes an RRS1 allele (RRS1 SLH1 ) with a single amino acid (leucine) insertion in the WRKY DNA-binding domain. Its poor growth due to constitutive defense activation is rescued at higher temperature. Transcription profiling data indicate that RRS1 SLH1 -mediated defense activation overlaps substantially with AvrRps4- and PopP2-regulated responses. To better understand the genetic basis of RPS4/RRS1-dependent immunity, we performed a genetic screen to identify   su ppressor of   s l h 1   i mmunity  ( sushi ) mutants. We show that many  sushi  mutants carry mutations in  RPS4 , suggesting that RPS4 acts downstream or in a complex with RRS1. Interestingly, several mutations were identified in a domain C-terminal to the RPS4 LRR domain. Using an  Agrobacterium -mediated transient assay system, we demonstrate that the P-loop motif of RPS4 but not of RRS1 SLH1  is required for RRS1 SLH1  function. We also recapitulate the dominant suppression of RRS1 SLH1  defense activation by wild type RRS1 and show this suppression requires an intact RRS1 P-loop. These analyses of RRS1 SLH1  shed new light on mechanisms by which NB-LRR protein pairs activate defense signaling, or are held inactive in the absence of a pathogen effector.

The Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in Arabidopsis thaliana