Article

Molecular and Cellular Biochemistry

, Volume 191, Issue 1, pp 51-58

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

  • Mette KuskAffiliated withBiokemisk Institut, Odense Universitet
  • , Rehana AhmedAffiliated withBiokemisk Institut, Odense Universitet
  • , Bo ThomsenAffiliated withThe Danish Institute of Animal Sciences, Research Center Foulum
  • , Christian BendixenAffiliated withThe Danish Institute of Animal Sciences, Research Center Foulum
  • , Olaf-Georg IssingerAffiliated withBiokemisk Institut, Odense Universitet
  • , Brigitte BoldyreffAffiliated withBiokemisk Institut, Odense Universitet

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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.

protein kinase CK2 subunit interaction two-hybrid screening p90rsk Doc-1 FAF1 IF-2mt propionyl CoA carboxylase