Project description:Genetic studies have shown essential functions of N-glycosylation during infection of the plant pathogenic fungi, however, systematic roles of N-glycosylation in fungi is still largely unknown. Biological analysis demonstrated N-glycosylated proteins were widely present at different development stages of Magnaporthe oryzae and especially strong in the appressorium and invasive hypha.A large-scale quantitative proteomics analysis was then performed to explore the roles of N-glycosylation in M. oryzae.
Project description:To investigate the role of iron excess in rice immune responses to Magnaporthe oryzae infection. Gene expression profiling analysis were performed using data obtained from RNA-seq of rice plants grown in differential iron supply and challenged with Magnaporthe oryzae spores.
Project description:This SuperSeries is composed of the following subset Series: GSE8517: Magnaporthe oryzae gene expression during biotrophic invasion of rice using version 2 of the Agilent Magnaporthe grisea Array (G4137B). GSE8518: Rice gene expression during biotrophic invasion by the rice blast fungus Magnaporthe oryzae using the Agilent Rice Array (G4138A). Keywords: SuperSeries Refer to individual Series
Project description:Concomitant sRNA and mRNAseq was carried out to elucidate the reprogramming occurring during Magnaporthe oryzae - Brachypodium distachyon interaction in three different setups: biotrophic stage of leaf infection (Leaf 2 DPI), necrotrophic stage of leaf infection (Leaf 4 DPI) and finally root infection (Root).
Project description:Concomitant sRNA and mRNAseq was carried out to elucidate the reprogramming occurring during Magnaporthe oryzae - Brachypodium distachyon interaction in three different setups: biotrophic stage of leaf infection (Leaf 2 DPI), necrotrophic stage of leaf infection (Leaf 4 DPI) and finally root infection (Root).
Project description:Rice blast caused by Magnaporthe oryzae is the most devastating disease of cultivated rice. Several protein kinase cascades have been known to be essential to pathogenesis or important for response to stress, mycelial growth and conidiation in M. oryzae. However, phosphoproteins and their phosphorylation sites (p-sites) in this important fungal pathogen remain largely to be identified. In this study, 8087 phosphopeptides corresponding to 9825 p-sites from 1147 phosphoproteins were identified in mycelia of M. oryzae under a false discovery rate of < 0.55% at the peptide level. Notably, 33 previously reported pathogenesis-related proteins were included in the phosphoproteins at the mascot delta score 10. Further analyses of 581 motif-containing phosphoproteins that met more stringent criteria revealed that the phosphoproteins shared 19 distinct phosphorylation motifs, including the motif RxxpSP that was newly identified in this study but is widely distributed in diverse organisms. These phosphoproteins were mapped into 81 biological pathways. A total of 82 acidic motif-containing phosphoproteins were identified. Surprisingly, none of them except one were mapped to any of the metabolic pathways. Furthermore, a prediction disclosed a total of 174 kinase-substrate specific interactions in mycelia of M. oryzae. This study also detected phosphorylation of the tyrosine phosphatase Pmp1 and 7 other proteins upstream of Pmk1, but not Pmk1 and its downstream transcription factors. These results prompted a necessary revision of Pmk1 MAPK cascade, in which dephosphorylation of Pmk1 by Pmp1 in mycelia may block the activation of downstream targets.
Project description:This SuperSeries is composed of the following subset Series: GSE36224: Comparison of transcript abundance in aerial mycelium of the Magnaporthe oryzae TRA1-deleted mutant and its parental strain GSE36225: Comparison of transcript abundance in ungerminated spores of the Magnaporthe oryzae TRA1-deleted mutant and its parental strain Refer to individual Series
Project description:We reported effects of Magnaporthe oryzae infection on expression of circRNA in the young leaves of the blast-resistant accession IRBLkm-Ts (IR25) and the blast-susceptible accession Lijiangxin Tuan Heigu (LTH)
