Premium
Analyzing Yeast Phosphorylation on a Global Scale to Probe Kinase‐Target Interactions
Author(s) -
Trinidad J.,
Burlingame A. L.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a978-b
Subject(s) - phosphorylation , yeast , saccharomyces cerevisiae , biochemistry , protein phosphorylation , kinase , gene , protein kinase a , biology , computational biology , chemistry , microbiology and biotechnology
Protein phosphorylation is fundamental to understanding the modulation of protein function. The Saccharomyces cerevisiae genome contains 122 unique protein kinases, and it has been estimated one third of all cellular proteins may be phosphorylated. IMAC was used to specifically purify phosphate‐containing peptides from whole cell tryptic digest. These phosphopeptides were fractionated by two‐dimensional chromatography and sequenced using a Q‐ToF mass spectrometer. This resulted in the identification of over 2000 phosphorylated peptides from approximately 1000 yeast proteins. These phosphorylated peptides spanned a range of biological processes as annotated in the Gene Ontology database. We performed motif scanning to identify both known and novel consensus motifs.