Host-adapted plant pathogens secrete numerous effectors into the host extracellular spaces or inside cells. The A. thaliana TNL receptor RPP1 confers strain-specific immunity through recognition of H.arabidopsidis effector ATR1. ATR1 consists of two ...
Host-adapted plant pathogens secrete numerous effectors into the host extracellular spaces or inside cells. The A. thaliana TNL receptor RPP1 confers strain-specific immunity through recognition of H.arabidopsidis effector ATR1. ATR1 consists of two alpha-helical domains that are involved in interactions with the receptor. The ATR1 N-terminal domain interacts with both, the C-terminal jelly roll/Ig-like domain (C-JID) and the LRRs of the RPP1 receptor [1].
Avirulence protein ATR1 is a secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants. It activates the N-terminal Toll-interleukin-1 receptor (TIR) domain of Arabidopsis NLR RPP1 [1]. This entry represents t ...
Avirulence protein ATR1 is a secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants. It activates the N-terminal Toll-interleukin-1 receptor (TIR) domain of Arabidopsis NLR RPP1 [1]. This entry represents the C-terminal helical domain, referred to as the WY-domain.
C-terminal jelly roll/Ig-like domain (C-JID) was defined in cryogenic electron microscopy (cryoEM) structures of plant intracellular immune receptors containing Toll/interleukin-1 receptor (TIR, PF01582), nucleotide-binding (NB-ARC, PF00931) and leuc ...
C-terminal jelly roll/Ig-like domain (C-JID) was defined in cryogenic electron microscopy (cryoEM) structures of plant intracellular immune receptors containing Toll/interleukin-1 receptor (TIR, PF01582), nucleotide-binding (NB-ARC, PF00931) and leucine-rich repeat (LRR) domains (TIR-NLRs) [1,2]. Structurally, the C-JID core is represented by a beta-sandwich made up of 8 to 9 beta-strands. C-JID matches the so-called post-LRR or C-terminal non-LRR domain detected earlier via MEME and BLAST searches [3,7]. The domain showed a strong distribution bias towards TIR-NLRs of dicotyledonous plant species despite broader taxonomic distribution of TIR-NLR in plant groups [1-7]. Structure-function analyses of cryoEM structures suggest that C-JID domains play a role in substrate recognition, such as binding to effector proteins from pathogens, and thus are involved in the initiation of signaling by TIR-NLR receptors [1,2]. Presence of C-JID (or post-LRR) and its importance for the function of Arabidopsis TIR-NLR RPS4 that partners with RRS1 for effector recognition suggest that C-JID has additional functions [4-6].