In eukaryotic cells, protein phosphorylation plays a key role in signal transduction and regulation. The kinases and phosphatases, which bring about reversible phosphorylation, account for up to 4% of the proteome and approximately one third of all eukaryotic proteins are phosphoproteins . We are studying the phosphoproteome in filamentous fungi, using A. nidulans as a model organism. Using cell lysate and affinity chromatographic resins (e.g., TiO2 ), we demonstrate selective enrichment of phosphopeptides. Using various software packages we have identified serine, threonine and tyrosine phosphorylation sites with high confidence. Furthermore, using synthetic phosphopeptides with an isobaric tagging reagent (DiART) we demonstrate a relatively inexpensive and robust method to perform quantitative phosphoproteomics.

Phosphoproteome profile of filamentous fungus Aspergillus nidulans

245th National Meeting (2013)

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