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Interactions of protein kinase CK2β subunit within the holoenzyme and with other proteins

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Abstract

Protein kinase CK2 is a ubiquitous, highly conserved protein kinase with a tetrameric α2β2 structure. For the formation of this tetrameric complex a β-β dimer seems to be a prerequisite. Using the two-hybrid system and a series of CK2β deletion mutants, we mapped domains involved in α-β and β-β interactions. We also detected an intramolecular b interaction within the amino acid stretch 132-165.

Using CK2β as a bait in a two-hybrid library screening several new putative cellular partners have been identified, among them the S6 kinase p90rsk, the putative tumor suppressor protein Doc-1, the Fas-associated protein FAF1, the mitochondrial translational initiation factor 2 and propionyl CoA carboxylase β subunit.

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Authors and Affiliations

  1. Biokemisk Institut, Odense Universitet, Campusvej 55, Odense, Denmark

    Mette Kusk, Rehana Ahmed, Olaf-Georg Issinger & Brigitte Boldyreff

  2. The Danish Institute of Animal Sciences, Research Center Foulum, P. 0. Box 39, Tjele, Denmark

    Bo Thomsen & Christian Bendixen

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  1. Mette Kusk
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  2. Rehana Ahmed
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  3. Bo Thomsen
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  4. Christian Bendixen
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  5. Olaf-Georg Issinger
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  6. Brigitte Boldyreff
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Kusk, M., Ahmed, R., Thomsen, B. et al. Interactions of protein kinase CK2β subunit within the holoenzyme and with other proteins. Mol Cell Biochem 191, 51–58 (1999). https://doi.org/10.1023/A:1006840613986

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