Phosphoproteome profile of Fusarium graminearum grown in vitro under nonlimiting conditions

Proteomics. 2012 Apr;12(7):1002-5. doi: 10.1002/pmic.201100065.

Abstract

This study presents a high-throughput proteomic analysis of phosphopeptides from Fusarium graminearum strain DAOM 233423 grown in vitro without nutritional limitation. Using a combination of strong cation exchange (SCX) and immobilized metal affinity chromatography (IMAC) followed by LC-MS, we identified 2902 putative phosphopeptides with homologous matches to 1496 different proteins. Functional classification of the annotated protein set revealed that phosphopeptides from nuclear proteins with ATP-binding function were the most abundant. There are indications that phosphorylation sites from well-characterized phosphoproteins representing diverse biological processes are conserved in F. graminearum: sequences of three phosphopeptides from known phosphoproteins (transcription elongation factor 1β, acidic ribosomal proteins, and glycogen synthase) revealed phosphorylation site conservation.

MeSH terms

  • Amino Acid Sequence
  • Fungal Proteins / analysis*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Fusarium / chemistry*
  • Fusarium / metabolism
  • Molecular Sequence Data
  • Phosphopeptides / analysis*
  • Phosphopeptides / chemistry
  • Phosphopeptides / metabolism
  • Phosphorylation
  • Proteome / analysis*
  • Proteome / chemistry
  • Proteome / metabolism
  • Proteomics
  • Sequence Alignment

Substances

  • Fungal Proteins
  • Phosphopeptides
  • Proteome