| Literature DB >> 26000484 |
Panagiotis F Sarris1, Zane Duxbury2, Sung Un Huh2, Yan Ma2, Cécile Segonzac3, Jan Sklenar2, Paul Derbyshire2, Volkan Cevik2, Ghanasyam Rallapalli2, Simon B Saucet2, Lennart Wirthmueller2, Frank L H Menke2, Kee Hoon Sohn3, Jonathan D G Jones4.
Abstract
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.Entities:
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Year: 2015 PMID： 26000484 DOI： 10.1016/j.cell.2015.04.024
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582