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Determination and mutational analysis of the phosphorylation site in the hypusine‐containing protein Hyp2p
Author(s) -
Klier Hannelore,
Wöhl Thorsten,
Eckerskorn Christoph,
Magdolen Viktor,
Lottspeich Friedrich
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80712-4
Subject(s) - serine , phosphorylation , biochemistry , gene isoform , threonine , phosphatase , enzyme , chemistry , saccharomyces cerevisiae , residue (chemistry) , biology , microbiology and biotechnology , yeast , gene
Electrospray mass spectrometry of the purified isoforms of the hypusine‐containing protein of Saccharomyces cerevisiae Hyp2p suggested a phosphorylation of the acidic isoform, which was confirmed by phosphatase treatment. The phosphorylation site was mapped to the N‐acetylated serine residue in position no. 1 by mass spectrometric analysis of enzymatic fragments. Mutation of this serine residue gives rise to only the basic isoform, confirming our protein chemical data. As this mutation has no effect on cell viability or growth rate, the unphosphorylated isoform is sufficient to exert the essential in vivo function of Hyp2p.