Fig. 3: BCG1-triggered plant immunity requires G/Q-rich domain.
a Representative N. benthamiana leaves showing cell death at 5 days post-inoculation (dpi) with Agrobacterium strains expressing indicated proteins under UV light. EV, empty vector. b Cell death intensity is indicated by the relative quantitative fluorescence intensity that is normalized to the INF1. Quantification was estimated with data obtained from twelve biologically independent samples. For the box plot, the center line indicates the median; the upper and lower bounds indicate the 75th and 25th percentiles, respectively; and the whiskers indicate the minimum and maximum. Different letters denote significant differences (p value < 0.01, one-way ANOVA) (upper panel). Western blot analysis showing the expressed proteins using the anti-HA antibody. Ponceau S staining serves as loading control (lower panel). c Dose–response curves of total ROS production induced by BCG1 protein in N. benthamiana leaf discs over 120 min. The values are the means ± standard deviation (SD) (n = 3, biologically independent experiments). d ROS production induced by 1 μM of indicated recombinant proteins in silenced N. benthamiana leaves. The values are the means ± SD (n = 3, biologically independent samples). e Relative expression of defense-related genes AtFRK1 and AtPR1 in leaves of Col-0 and bak1 bkk1 cerk1 (bbc) mutant plants of A. thaliana was evaluated by RT-qPCR using ACTIN2 gene as the internal control. Values represent the means ± SD (n = 3, biologically independent experiments). Different letters denote significant differences (p value < 0.01, one-way ANOVA). P values for (b, e) are shown in the Source Data. f ROS burst induced by 1 μM of indicated recombinant proteins in Col-0 and bbc mutant leaves of A. thaliana. The values are the means ± SD (n = 3, biologically independent samples). g–h GFP- or HA-tagged BCG1, BCG1E118A, BCG1ΔGQ, and BCG1ΔGQ/E118A was co-expressed with HA- or GFP-tagged NbBAK1 and NbSORIR1 in N. benthamiana leaves. Co-IP assays were performed using GFP-trap A beads and the indicated proteins were immunoblotted with anti-HA and anti-GFP antibodies, respectively. Source data are provided as a Source Data file.
