Extended Data Fig. 1: The N-myristoylation motif is a common feature of Arabidopsis CNLs without a MADA motif.
From: Assembly of helper NLR resistosome clusters upon activation of a coiled-coil NLR
a, Domain architecture of a canonical CNL protein indicating the locations of the MADA and MGxxxS/T motifs. Consensus sequence logos generated by MEME and corresponding alignments are shown for the MADA motif (NRC4, ZAR1) and the MGxxxS/T motif (SUMM2, RPS5). b, The α1 helix of active ZAR1 resistosome (PDB ID: 6J5T), but not inactive ZAR1 (PDB ID: 6J5W), protrudes into the PM. The membrane (gray, spheres) targeting was modeled by PPM 3.0, and images were created using PyMOL. c, The α1 helix of SUMM2 and RPS5 coiled-coil (CC) domains is anchored to the PM. The structures of SUMM2 (P60838) and RPS5 (O64973) CC domains were predicted by AlphaFold2, and the membrane targeting was modeled by PPM 3.0. d, Phylogenetic analysis of CC domains (amino acids 1–160) of Arabidopsis 41 CNLs and 5 RNLs divides them into three subgroups. Amino acid sequences of N-terminal domains were aligned using ClustalW. The phylogenetic tree was constructed via the NJ method with 1000 bootstrap values in MEGA7. Arabidopsis CNLs were divided into MADA CNL (CC-NLR), MGxxxS/T CNL (CCG10-NLR), and Helper RNL (CCR-NLR) subgroups.
