Understanding and engineering immune receptor complexes in plants.
Z. DUXBURY (1), S. Huh (2), P. Ding (2), Y. Ma (2), J. Sklenar (2), F. Menke (2), P. Sarris (3), J. Jones (2) (1) The Sainsbury Laboratory, United Kingdom; (2) The Sainsbury Laboratory, United Kingdom; (3) University of Exeter, United Kingdom

Nucleotide-binding domain and Leucine-rich Repeat-containing (NLR) proteins are the major class of intracellular receptors that confer resistance to pathogens in plants. The ability of NLRs to recognise and respond to secreted pathogen molecules (“effectors”) is dependent on the formation of protein complexes. There is relatively little known about the molecular mechanisms that transduce the immune signal from an active NLR to the nucleus to initiate the transcriptional reprogramming required for an effective immune response. The NLR RRS1 contains a WRKY DNA-binding domain and has been hypothesised to directly reprogram the transcriptional machinery during an immune response. Our lab and others have demonstrated that this WRKY DNA-binding domain is acting as bait for pathogen effectors and may not be responsible for direct transcriptional regulation. RRS1 requires both intramolecular and intermolecular interactions to establish an immune signal in cooperation with a partner NLR, called RPS4. In order to fully characterise downstream signalling requirements, we have established stable Arabidopsis lines carrying epitope-tagged RRS1 and RPS4 for a forward proteomics analysis. I will discuss protein components required for signalling-competent RRS1 and RPS4 complexes. Understanding NLR receptor complexes will provide insight into positive and negative regulation of immune responses and allow us to more effectively engineer disease immunity into disease-susceptible plants.

Abstract Number: C9-6, P17-656
Session Type: Concurrent