Extended Data Fig. 10: Plant Holliday junction resolvase also can inhibit the biofilms of pathogenic bacteria.
a, The full-length amino acid sequences of Holliday junction resolvases from several pathogenic bacteria and plants were used to generate the phylogenetic tree by the Neighbor-Joining method. The MOC1 homologous proteins in different crops are highlighted in green and the RuvC homologous proteins in a variety of pathogenic bacteria are highlighted in blue. ComEA, a membrane-bound high-affinity DNA-binding receptor in Bacillus atrophaeus, was selected as an outgroup. The above experiments were repeated three times with similar results. b, Schematic ___domain structure of MOC1. Sl, Solanum lycopersicum; Os, Oryza sativa. The signal peptide is predicted by InterPro or SignalP-5.0. c, Purified His-SlMOC1 and His-OsMOC1 fusion proteins from E. coli were separated by SDS-PAGE. Expression was induced by IPTG and purified by affinity chromatography with Ni-NTA agarose beads. The chloroplast transit peptide was removed during protein expression. d and e The general biofilm-inhibitory function of plant MOC1 proteins towards pathogenic bacteria. The purified His-SlMOC1 inhibits the biofilm formed by PXO99A, and His-OsMOC1 disrupts the biofilm generated by GMI1000. Biofilms were stained with crystal purple and imaged in the PCR tubes. Data are presented as mean values ± SD (n=6 biological replicates). Statistically significant differences in d and e are indicated by different lowercase letters (One-way ANOVA, P < 0.05). The above experiments were repeated three times with similar results.
