A Plant Immune Receptor Detects Pathogen Effectors that Target WRKY Transcription Factors

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...

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Bibliographic Details
Published in:Cell 2015-05, Vol.161 (5), p.1089-1100
Main Authors: Sarris, Panagiotis F., Duxbury, Zane, Huh, Sung Un, Ma, Yan, Segonzac, Cécile, Sklenar, Jan, Derbyshire, Paul, Cevik, Volkan, Rallapalli, Ghanasyam, Saucet, Simon B., Wirthmueller, Lennart, Menke, Frank L.H., Sohn, Kee Hoon, Jones, Jonathan D.G.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Arabidopsis - immunology
Arabidopsis - microbiology
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - metabolism
Bacterial Proteins - immunology
Immunity, Innate
Molecular Sequence Data
Nicotiana - immunology
Nicotiana - microbiology
Plant Proteins - metabolism
Protein Structure, Tertiary
Pseudomonas fluorescens - metabolism
Pseudomonas fluorescens - pathogenicity
Pseudomonas syringae - immunology
Pseudomonas syringae - metabolism
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Summary: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. [Display omitted] •A plant immune receptor detects two different bacterial effectors via a WRKY domain•One pathogen effector PopP2 acetylates lysines and another, AvrRps4 binds the WRKY domain•This regulation occurs for other plant WRKY proteins involved in immunity•Receptor WRKY domain enables detection of effectors that target such proteins An Arabidopsis intracellular immune receptor complex, one component of which contains A WRKY DNA binding domain, detects specific bacterial effectors to activate defense. Acetylation of WRKY domains by an effector likely interferes with host defense and this domain in the receptor complex enables detection of pathogen effectors that broadly target WRKY domain proteins.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2015.04.024