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Fig. 7 | Phytopathology Research

Fig. 7

From: A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

Fig. 7

Both the RRM and the first two RGG motifs are essential for the full function of MoGrp1. a Structure diagram of N-terminal 3 × Flag tagged MoGrp1 (cg1f), C-terminal GFP tagged MoGrp1 (cg1g) and their mutated alleles, including RNP-2 deletion (dRRM, MoGrp1Δ119–125), N-terminal deletion (dN, MoGrp1Δ1–74), glycine-rich domain complement transformant (dNR, MoGrp1Δ1–173), deletion from the 3rd RGG motif to the end (Δ265–324, MoGrp1Δ265–324), deletion from the 2nd RGG motif to the end (Δ191–324, MoGrp1Δ191–324), deletion from the 1st RGG motif to the end (Δ182–324, MoGrp1Δ182–324), deletion from 182 to 190 aa (Δ182–190, MoGrp1Δ182–190), transformant containing RRM and 1st RGG (dNG, MoGrp175–190), and AGG mutant (AGG, MoGrp1R182A, R191A); b Pathogenicity test of diverse domain-complemented strains in rice seedlings. Typical disease lesions were photographed at 5–7 dpi; c Colony diameter of diverse domain-complemented strains on OTA plates at 28 °C for 5 days. The mean ± SD was calculated based on three independent experiments measuring three plates in each replicate. *P < 0.05; d Conidiation capacity of diverse domain-complemented strains on OTA plates. The mean ± SD was calculated based on three independent experiments with measuring three plates in each replicate. *P < 0.05

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