Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2

Rafał Zieliński; Ulf Hellman; Konrad Kubiński; Ryszard Szyszka

doi:10.1007/s11010-005-9104-4

Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2

Rafał Zieliński, Ulf Hellman, Konrad Kubiński, Ryszard Szyszka

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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′ (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.

Original language	English (US)
Pages (from-to)	191-197
Number of pages	7
Journal	Molecular and Cellular Biochemistry
Volume	286
Issue number	1-2
DOIs	https://doi.org/10.1007/s11010-005-9104-4
State	Published - Jun 2006
Externally published	Yes

Keywords

Cleavage/polyadenylation factor complex
Fip1
Mass spectrometry
Polyadenylation
Protein kinase CK2
Yeast

ASJC Scopus subject areas

Molecular Biology
Clinical Biochemistry
Cell Biology

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10.1007/s11010-005-9104-4

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title = "Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2",

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.",

keywords = "Cleavage/polyadenylation factor complex, Fip1, Mass spectrometry, Polyadenylation, Protein kinase CK2, Yeast",

author = "Rafa{\l} Zieli{\'n}ski and Ulf Hellman and Konrad Kubi{\'n}ski and Ryszard Szyszka",

note = "Funding Information: This work was supported by a research grants from Ministry of Education and Science (PBZ-MIN-014/P05/2004) and from Catholic University of Lublin.",

year = "2006",

month = jun,

doi = "10.1007/s11010-005-9104-4",

language = "English (US)",

volume = "286",

pages = "191--197",

journal = "Molecular and Cellular Biochemistry",

issn = "0300-8177",

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TY - JOUR

T1 - Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2

AU - Zieliński, Rafał

AU - Hellman, Ulf

AU - Kubiński, Konrad

AU - Szyszka, Ryszard

N1 - Funding Information: This work was supported by a research grants from Ministry of Education and Science (PBZ-MIN-014/P05/2004) and from Catholic University of Lublin.

PY - 2006/6

Y1 - 2006/6

N2 - 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.

AB - 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.

KW - Cleavage/polyadenylation factor complex

KW - Fip1

KW - Mass spectrometry

KW - Polyadenylation

KW - Protein kinase CK2

KW - Yeast

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U2 - 10.1007/s11010-005-9104-4

DO - 10.1007/s11010-005-9104-4

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SN - 0300-8177

VL - 286

SP - 191

EP - 197

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

IS - 1-2

ER -

Fip1 - An essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2

Abstract

Keywords

ASJC Scopus subject areas

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