Molecular and Cellular Biochemistry

, 286:191

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

Authors

  • Rafał Zieliński
    • Department of Molecular Biology, Environmental Protection InstituteCatholic University of Lublin
  • Ulf Hellman
    • Ludwig Institute for Cancer Research
  • Konrad Kubiński
    • Department of Molecular Biology, Environmental Protection InstituteCatholic University of Lublin
    • Department of Molecular Biology, Environmental Protection InstituteCatholic University of Lublin
Article

DOI: 10.1007/s11010-005-9104-4

Cite this article as:
Zieliński, R., Hellman, U., Kubiński, K. et al. Mol Cell Biochem (2006) 286: 191. doi:10.1007/s11010-005-9104-4

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

yeastprotein kinase CK2polyadenylationcleavage/polyadenylation factor complexFip1mass spectrometry
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Copyright information

© Springer Science+Business Media, Inc. 2005