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Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins.

Protein kinase CK2 is a ubiquitous, highly conserved protein kinase with a tetrameric alpha2beta2 structure. For the formation of this tetrameric complex a beta-alpha dimer seems to be a prerequisite. Using the two-hybrid system and a series of CK2beta deletion mutants, we mapped domains involved in alpha-beta and beta-beta interactions. We also detected an intramolecular beta interaction within the amino acid stretch 132-165. Using CK2beta 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 beta subunit.[1]

References

  1. Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins. Kusk, M., Ahmed, R., Thomsen, B., Bendixen, C., Issinger, O.G., Boldyreff, B. Mol. Cell. Biochem. (1999) [Pubmed]
 
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