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MGG1 (Magnaporthe oryzae G protein gamma subunit) putatively encodes a 93-amino-acid protein with a typical G-protein gamma like domain (GGL) and C-terminal CAAX box and has been previously identified and characterized by T-DNA insertional mutagenesis.The amino-acid sequence of Mggl is highly identical to the homologues of other filamentous fungi.Here the Magnaporthe MGG1 was further characterized by the strategy of targeted gene replacement and complementation.The results showed that the gene deletion mutants (△mggl) were defective in conidition, fertility, appressorium formation and pathogenicity, which were similar to the previous insertional mutant A1-412.Moreover, the defect of appressorium formation of the mutants could be partially restored by adding exgenous cAMP or IBMX(3-iso-butyl-1-methylxanthin), although the induced appressoria were still nonfunctional.Analysis of Mggl N-terminal GFP tagging showed Mgg1 was mainly localized in cytoplasmic membrane.All phenotypes of △mgg1 mutants were complemented by reintroduction of the gene containing 3-untranslated region (UTR), but were not restored without 3UTR, indicating MGG1 3UTR sequence might be necessary for full function of the gene.Taken together, MGG1 is required for conidition, fertility, appressorium formation and pathogenicity in M.oryzae.