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A Plant Immune Receptor Detects Pathogen Effectors that Target WRKY Transcription Factors
Sarris, Panagiotis F.,Duxbury, Z.,Huh, S.,Ma, Y.,Segonzac, C.,Sklenar, J.,Derbyshire, P.,Cevik, V.,Rallapalli, G.,Saucet, Simon B.,Wirthmueller, L.,Menke, Frank L.H.,Sohn, K.,Jones, Jonathan D.G. Cell Press ; MIT Press 2015 Cell Vol.161 No.5
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.
Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor
Williams, Simon J.,Sohn, Kee Hoon,Wan, Li,Bernoux, Maud,Sarris, Panagiotis F.,Segonzac, Cecile,Ve, Thomas,Ma, Yan,Saucet, Simon B.,Ericsson, Daniel J.,Casey, Lachlan W.,Lonhienne, Thierry,Winzor, Dona American Association for the Advancement of Scienc 2014 Science Vol.344 No.6181
<P><B>Universal Immune Function</B></P><P>Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of <I>Arabidopsis</I> receptors, <B>Williams <I>et al.</I></B> (p. 299; see the Perspective by <B>Nishimura and Dangl</B>) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest the molecular mechanisms may translate broadly.</P>