Necrosis inducing protein-1 (NIP1) is a small phytotoxic protein secreted by the barley pathogen Rhynchosporium secalisconsists. It is a fungal avirulence protein on host plants of the Rrs1 resistance genotype []. NIP1 consists of two parts containing β-sheets of two and three anti-parallel strands, respectively. Five intramolecular disulphide bonds stabilise these parts and their position with respect to each other, providing a high level of stability [].
Necrosis inducing protein-1 (NIP1) is a small phytotoxic protein secreted by the barley pathogen Rhynchosporium secalisconsists. It is a fungal avirulence protein on host plants of the Rrs1 resistance genotype []. NIP1 consists of two parts containing β-sheets of two and three anti-parallel strands, respectively. Five intramolecular disulphide bonds stabilise these parts and their position with respect to each other, providing a high level of stability [].
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), nucleotide-binding (NB-ARC) and leucine-rich repeat (LRR) domains (TIR-NLRs) [, ]. Structurally, the C-JID core is represented by a β-sandwich made up of 8 to 9 β-strands. C-JID matches the so-called post-LRR or C-terminal non-LRR domain detected earlier via MEME and BLAST searches [, ]. The domain showed a strong distribution bias towards TIR-NLRs of dicotyledonous plant species despite broader taxonomic distribution of TIR-NLR in plant groups [, ]. 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 signalling by TIR-NLR receptors [, ]. 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 [, , ].
