Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold
Fig 3
Mutation of conserved residues of the N-terminal region of NWD2 affect [Het-s]-inducing activity of chimeric nwd2 alleles.
A. An homology model of the NWD2(3–23) region based on the HET-s(218–289) β-solenoid fold (after [24]) is given together with a graphical representation of the structure of the two repeats of the HET-s PFD (after [18,19]). B. Comparison of the sequence conservation in repeats 1 and 2 of HET-s homologs (noted r1 and r2) and NWD2 homologs found in various pezizomycotina (noted r0). The consensus sequences were generated using MEME; the size of the letter reflects conservation; scale is given in informational content measured in bits. C. Alignment of the HET-s-like motif from NWD2 homologs found in various pezizomycotina. The NWD2 sequence is boxed in red. D. [Het-s]-inducing activity of wild-type and mutated nwd2e1 alleles in a ΔPaHsp104 het-c2 background. Experiments have been carried out at least in triplicate and error bars are standard deviations; the asterisks denote that prion conversion rate was zero.