Extended Data Fig. 3: Gas2 from multiple rice fungal pathogens interacts with SnRK1β1A.
From: Inactivating SnRK1β1A promotes broad-spectrum disease resistance in rice
a, The alignment of Arabidopsis AKINβ1, rice SnRK1β1A, SnRK1β1B, SnRK1β1C and SnRK1β3. Lines indicate the CBM domain and βCTD domain, and asterisks indicate the conserved lysine residues in rice SnRK1 β subunits that may serve as potential ubiquitination sites. b, Y2H assays showing interaction of Gas2 with the CTD domain of SnRK1β1A. The curve in the N-terminal indicates potential myristoylated glycine (G), the blue and green boxes indicate the CBM and CTD domains, respectively. c, Y2H assays showing interaction of SnRK1β1A with DUF3129 domain of Gas2. The blue box and the orange box indicate the DUF3129 domain and the β-strand of Gas2, respectively. d, LCI assays showing the interaction of SnRK1β1A with Gas2 from M. oryzae. The relative luciferase activity was measured, and protein expression was confirmed by immunoblot analysis with anti-HA and anti-cluc antibodies. e, Y2H assays showing interaction of SnRK1β1A with Gas2 from M. oryzae, but neither with Gas2-like proteins from M. oryzae and B. oryzae nor with unrelated MAS proteins from N. crassa. f, LCI assays showing the interaction of SnRK1β1A with Gas2 from B. oryzae, U. virens, R. solani, F. fujikuroi and F. graminearum, but not with the Gas2-like protein from B. oryzae nor with unrelated MAS proteins from N. crassa. The relative luciferase activity was measured, and protein expression was confirmed by immunoblot analysis with anti-HA and anti-cluc antibodies. Data represent mean ± s.d.; n = biologically independent samples in the graphs. Experiments were repeated at least three times (b–f) with similar results. RLU, relative luminescence units.
