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Phosphoproteome profile of F usarium graminearum grown in vitro under nonlimiting conditions
Author(s) -
Rampitsch Christof,
Tinker Nicholas A.,
Subramaniam Rajagopal,
BarkowOesterreicher Simon,
Laczko Endre
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100065
Subject(s) - phosphorylation , ribosomal protein , chemistry , in vitro , biochemistry , elongation factor , microbiology and biotechnology , biology , rna , gene , ribosome
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.