title: Phosphoproteome profile of Fusarium graminearum grown in vitro under nonlimiting conditions.
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.
authors.affiliation: Agriculture and Agrifood Canada, Winnipeg, Manitoba, Canada. chris.rampitsch@agr.gc.ca
authors.forename: Christof
authors.initials: C
authors.lastname: Rampitsch
authors.forename: Nicholas A
authors.initials: NA
authors.lastname: Tinker
authors.forename: Rajagopal
authors.initials: R
authors.lastname: Subramaniam
authors.forename: Simon
authors.initials: S
authors.lastname: Barkow-Oesterreicher
authors.forename: Endre
authors.initials: E
authors.lastname: Laczko
mesh_terms: D000595:Amino Acid Sequence; D005656:Fungal Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D005670:Fusarium / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D020543:Proteome / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D040901:Proteomics; D016415:Sequence Alignment
chemical_list: D005656:Fungal Proteins; D010748:Phosphopeptides; D020543:Proteome