Fip1 — an Essential Component of the Saccharomyces Cerevisiae Polyadenylation Machinery is Phosophorylated by Protein Kinase CK2

  • Rafał Zieliński
  • Ulf Hellman
  • Konrad Kubiński
  • Ryszard Szyszka
Article

Abstract

Since Fip1 is phosphoprotein we investigated whether it is a substrate for protein kinase CK2. According to the amino acid sequence Fip1 harbours twenty putative CK2 phosphorylation sites. Here we have report characterization of Fip1 as a substrate for both forms of CK2. Fip1 serves as a substrate for both the recombinant CK2α ′ (Km 1.28 μM) and holoenzyme (Km 1.4 μM) but not for CK1. By MALDI-MS we identified the two serine residues at positions 73 and 77 as the possible in vitro phosphorylation sites. These data may help to elucidate the role of Fip1 in the mRNA 3'-OH polyadenylation process and the involvement of CK2 mediated phosphorylation in regulation of interactions and activity members of cleavage/polyadenylation factor (CPF) complex.

Key words

yeast protein kinase CK2 polyadenylation cleavage/polyadenylation factor complex Fip1 mass spectrometry 

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Copyright information

© Springer Science+Business Media, Inc. 2005

Authors and Affiliations

  • Rafał Zieliński
    • 1
  • Ulf Hellman
    • 2
  • Konrad Kubiński
    • 1
  • Ryszard Szyszka
    • 1
  1. 1.Department of Molecular Biology, Environmental Protection InstituteCatholic University of LublinLublinPoland
  2. 2.Ludwig Institute for Cancer ResearchUppsalaSweden

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