A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization
Fig 4
Mg1LysM sequence polymorphisms in Z. tritici.
(A) Five non-synonymous SNPs were identified in 149 Z. tritici strains from four different populations. Arrows indicate the position of the residues involved in the formation of salt bridges, while green underlining indicates the signal peptide and red underlining the chitin-binding loops. Red and green underlines indicate the signal peptide and the chitin binding sites, respectively. (B) While the mutations (shown in blue sticks) do not co-localize but occur dispersed over the Mg1LysM protein, none of them is in the chitin-binding site or in the (homo-)dimerization surface. (C) Mg1LysM and the two allelic variants Mg1LysM_1E4 and Mg1LysM-3F4 bind insoluble chitin. All proteins were heterologously produced in E. coli and incubated with chitin for 6 hours. After centrifugation, pellets and supernatants were analysed on polyacrylamide gel followed by CBB staining.