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PXD002364

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2017-07-17
  • AnnouncementXML: Submission_2017-07-17_06:11:06.xml
  • DigitalObjectIdentifier: http://dx.doi.org/10.6019/PXD002364
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Supported dataset by repository
  • PrimarySubmitter: Ruijin Wang
  • Title: Phosphoproteome of Magnaporthe oryzae
  • 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.
  • SpeciesList: scientific name: Magnaporthe oryzae (strain P131) (Rice blast fungus) (Pyricularia oryzae); NCBI TaxID: 1143193;
  • ModificationList: monohydroxylated residue: 15.994915; phosphorylated residue: 79.966331; iodoacetamide derivatized residue: 57.021464
  • Instrument: amaZon Speed ETD

Dataset History

VersionDatetimeStatusChangeLog Entry
02015-06-12 01:12:21ID requested
12017-07-17 06:11:07announced

Publication List

  1. Wang R, Peng J, Li QX, Peng YL, Phosphorylation-Mediated Regulatory Networks in Mycelia of Pyricularia oryzae Revealed by Phosphoproteomic Analyses. Mol Cell Proteomics, ():(2017) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: Rice blast fungus, phosphorylation, mycelium, pathogensis

Contact List

    Qing X. Li
    • contact affiliation: Department of Molecular Biosciences and Bioengineering, University of Hawaii at Manoa, Honolulu, Hawaii 96822, USA
    • contact email: qingl@hawaii.edu
    • lab head:
    Ruijin Wang
    • contact affiliation: University of Hawaii/ China Agricultural University
    • contact email: wrjtjbd@gmail.com
    • dataset submitter:

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