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Fip1 - an essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research.
2006 (English)In: Molecular and Cellular Biochemistry, ISSN 0300-8177, E-ISSN 1573-4919, Vol. 286, no 1-2, 191-197 p.Article in journal (Refereed) Published
Abstract [en]

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 ′ (K m 1.28 μM) and holoenzyme (K m 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.

Place, publisher, year, edition, pages
2006. Vol. 286, no 1-2, 191-197 p.
Keyword [en]
Yeast, protein kinase CK2, polyadenylation, cleavage/polyadenylation factor complex, Fip1, mass spectrometry
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-80954DOI: 10.1007/s11010-005-9104-4PubMedID: 16496213OAI: oai:DiVA.org:uu-80954DiVA: diva2:108868
Available from: 2006-07-05 Created: 2006-07-05 Last updated: 2017-12-14Bibliographically approved

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Hellman, Ulf

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