Mutation of conserved residues of the N-terminal region of NWD2 affect [Het-s]-inducing activity of chimeric <i>nwd2</i> alleles.

<p>A. An homology model of the NWD2(3–23) region based on the HET-s(218–289) β-solenoid fold (after [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1002059#pbio.1002059.ref024" target="_blank">24</a>]) is given together with a graphical representation of the structure of the two repeats of the HET-s PFD (after [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1002059#pbio.1002059.ref018" target="_blank">18</a>,<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1002059#pbio.1002059.ref019" target="_blank">19</a>]). 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 <i>nwd2</i>^e1 alleles in a <i>ΔPaHsp104 het-c2</i> 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.