Yeast Elf1 factor is phosphorylated and interacts with protein kinase CK2

Konrad Kubinski; Rafal Zielinski; Ulf Hellman; Elzbieta Mazur; Ryszard Szyszka

doi:10.5483/bmbrep.2006.39.3.311

Yeast Elf1 factor is phosphorylated and interacts with protein kinase CK2

Konrad Kubinski, Rafal Zielinski, Ulf Hellman, Elzbieta Mazur, Ryszard Szyszka

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

9 Scopus citations

Abstract

One of the biggest group of proteins influenced by protein kinase CK2 is formed by factors engaged in gene expression. Here we have reported recently identified yeast transcription elongation factor Elf1 as a new substrate for both monomeric and tetrameric forms of CK2. Elf1 serves as a substrate for both the recombinant CK2α′ (K_m 0.38 μM) and holoenzyme (K_m 0.13 μM). By MALDI-MS we identified the two serine residues at positions 95 and 117 as the most probable in vitro phosphorylation sites. Co-immunoprecypitation experiments show that Elf1 interacts with catalytic (α and α′) as well as regulatory (β and β′) subunits of CK2. These data may help to elucidate the role of protein kinase CK2 and Elf1 in the regulation of transcription elongation.

Original language	English (US)
Pages (from-to)	311-318
Number of pages	8
Journal	Journal of Biochemistry and Molecular Biology
Volume	39
Issue number	3
DOIs	https://doi.org/10.5483/bmbrep.2006.39.3.311
State	Published - 2006
Externally published	Yes

Keywords

Cloning and overexpression
Mass spectrometry
Phosphorylation
Protein kinase CK2
Protein-protein interaction
Transcription
Transcription factor Elf1
Yeast

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.5483/bmbrep.2006.39.3.311

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title = "Yeast Elf1 factor is phosphorylated and interacts with protein kinase CK2",

abstract = "One of the biggest group of proteins influenced by protein kinase CK2 is formed by factors engaged in gene expression. Here we have reported recently identified yeast transcription elongation factor Elf1 as a new substrate for both monomeric and tetrameric forms of CK2. Elf1 serves as a substrate for both the recombinant CK2α′ (Km 0.38 μM) and holoenzyme (Km 0.13 μM). By MALDI-MS we identified the two serine residues at positions 95 and 117 as the most probable in vitro phosphorylation sites. Co-immunoprecypitation experiments show that Elf1 interacts with catalytic (α and α′) as well as regulatory (β and β′) subunits of CK2. These data may help to elucidate the role of protein kinase CK2 and Elf1 in the regulation of transcription elongation.",

keywords = "Cloning and overexpression, Mass spectrometry, Phosphorylation, Protein kinase CK2, Protein-protein interaction, Transcription, Transcription factor Elf1, Yeast",

author = "Konrad Kubinski and Rafal Zielinski and Ulf Hellman and Elzbieta Mazur and Ryszard Szyszka",

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AU - Kubinski, Konrad

AU - Zielinski, Rafal

AU - Hellman, Ulf

AU - Mazur, Elzbieta

AU - Szyszka, Ryszard

PY - 2006

Y1 - 2006

N2 - One of the biggest group of proteins influenced by protein kinase CK2 is formed by factors engaged in gene expression. Here we have reported recently identified yeast transcription elongation factor Elf1 as a new substrate for both monomeric and tetrameric forms of CK2. Elf1 serves as a substrate for both the recombinant CK2α′ (Km 0.38 μM) and holoenzyme (Km 0.13 μM). By MALDI-MS we identified the two serine residues at positions 95 and 117 as the most probable in vitro phosphorylation sites. Co-immunoprecypitation experiments show that Elf1 interacts with catalytic (α and α′) as well as regulatory (β and β′) subunits of CK2. These data may help to elucidate the role of protein kinase CK2 and Elf1 in the regulation of transcription elongation.

AB - One of the biggest group of proteins influenced by protein kinase CK2 is formed by factors engaged in gene expression. Here we have reported recently identified yeast transcription elongation factor Elf1 as a new substrate for both monomeric and tetrameric forms of CK2. Elf1 serves as a substrate for both the recombinant CK2α′ (Km 0.38 μM) and holoenzyme (Km 0.13 μM). By MALDI-MS we identified the two serine residues at positions 95 and 117 as the most probable in vitro phosphorylation sites. Co-immunoprecypitation experiments show that Elf1 interacts with catalytic (α and α′) as well as regulatory (β and β′) subunits of CK2. These data may help to elucidate the role of protein kinase CK2 and Elf1 in the regulation of transcription elongation.

KW - Cloning and overexpression

KW - Mass spectrometry

KW - Phosphorylation

KW - Protein kinase CK2

KW - Protein-protein interaction

KW - Transcription

KW - Transcription factor Elf1

KW - Yeast

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SN - 1225-8687

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JO - Journal of Biochemistry and Molecular Biology

JF - Journal of Biochemistry and Molecular Biology

IS - 3

ER -

Yeast Elf1 factor is phosphorylated and interacts with protein kinase CK2

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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