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Genome-wide mapping of a repressive H3K36me2 reader during growth mycelia in the Magnaporthe oryzae

ABSTRACT: A putative EAF3/MRG15 ortholog N1617, containing chromo and MRG domain, is a partner of Ash1 in Magnaporthe oryzae

ORGANISM(S): Pyricularia oryzae

PROVIDER: GSE246678 | GEO | 2023/11/29

REPOSITORIES: GEO

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Next Generation Sequencing of a repressive H3K36me2 reader during growth mycelia in the Magnaporthe oryzae

Project description:A putative EAF3/MRG15 ortholog N1617, containing chromo and MRG domain, is a partner of Ash1 in Magnaporthe oryzae

2023-11-29 | GSE246677 | GEO

Identification of Ash1 and N1617 interactors in Magnaporthe oryzae

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Mrg15 allosterically activates Ash1’s H3K36 methyltransferase activity and facilitates Ash1’s trithorax group protein function in Drosophila

Project description:Ash1 is a classic Trithorax group protein possessing an H3K36-specific histone methyltransferase activity. Ash1 plays a critical role in antagonizing Polycomb silencing and its loss-of-function mutations lead to inactivation of certain Hox genes and homeotic transformation. Here, we report the purification of Ash1 complex with the identification of two novel subunits, Mrg15 and Nurf55. Interestingly, Mrg15 stimulates the enzymatic activity of Ash1 in vitro, and such stimulation is independent of the chromo domain of Mrg15. In vivo, Mrg15 is recruited by Ash1 to their common target genes and Mrg15 is essential for the proper deposition of H3K36me2 at these regions.

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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.

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Iron treatment induces resistance against the rice blast fungus Magnaporthe oryzae through potentiation of immune responses

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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

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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.

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CircRNAs function as a new layer of regulation in rice-Magnaporthe oryzae interaction

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