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Fig. 4 | Phytopathology Research

Fig. 4

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

Fig. 4

MoGrp1 is localized to nuclei and binds to poly(U) RNA. a MoGrp1 is localized to nuclei of conidia, appressoria, and infection hyphae of strain cg1g expressing a MoGrp1-GFP fusion protein. Bar, 20 μm; b Relative expression levels of MoGRP1 in mycelia (My), conidium (Co), mature appressorium (Ap12h), and invasive hyphae (IH24h and IH42h) measured by quantitative RT-PCR. The expression level of MoGRP1 was first normalized with the actin gene in each tested tissue, and the expression level of MoGRP1 was set to 1. The means and standard deviations were calculated based on two independent experiments with three replicates; c The 3 × Flag-MoGrp1 or 3 × Flag-MoGrp1ΔRNP-2 constructs bind to different types of biotinylated nucleic acids, including poly(U)30, poly(A)30, single-strand DNA (ssDNA), and double-strand DNA (dsDNA). The 3 × Flag-tagged protein was immunoprecipitated from strain cg1f expressing the 3 × Flag-MoGrp1 fusion protein or strain cg1fdR expressing the 3 × Flag- MoGrp1ΔRNP-2 fusion protein. (−) is a negative control, showing that beads cannot bind target proteins without biotinylated nucleic acids

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