Determination and mutational analysis of the phosphorylation site in the hypusine-containing protein Hyp2p.

@article{Klier1993DeterminationAM,
  title={Determination and mutational analysis of the phosphorylation site in the hypusine-containing protein Hyp2p.},
  author={Hannelore Klier and Thorsten W{\"o}hl and Christoph Eckerskorn and Viktor Magdolen and Friedrich Lottspeich},
  journal={FEBS letters},
  year={1993},
  volume={334 3},
  pages={360-4}
}
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… CONTINUE READING

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