Figure 7

Identification of a 30 amino acids necrosis inducing peptide in the Xyn11A surface. A) Alignment of a short region (residues 131 to 160 in the immature protein) on the enzyme surface for B. cinerea Xyn11A (Bc) and the two other xylanases with necrosis inducing activity: T. reesei xylanase II (Tr) and T. viride EIX (Tv). Previously reported necrosis-inducing region (purple) and a well conserved contiguous region (blue) are indicated. The whole shown region was expressed in E. coli. B) Amino acids having a frequency of more than 10%, at their respective positions, in the alignment of 308 family-11 glycosyl hydrolases downloaded from Pfam. C) Percentage frequency on the alignment of the residues indicated in (B). D) Predicted 3D structure for Xyn11A showing (green, purple, and blue) the two beta sheets expressed in E. coli and the two Glu residues in the active site (red). E) Necrosis inducing activity of the 30-amino acids peptide expressed in E. coli by itself (EliX), fused to the C terminus of GFP (GFP-EliX), or fused to its N terminus (EliX-GFP). Controls were made with the whole Xyn11A, GFP alone, or buffer. Picture was taken 3 days after infiltration.