Molecular and Cellular Biochemistry

, Volume 191, Issue 1–2, pp 51–58 | Cite as

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

  • Mette Kusk
  • Rehana Ahmed
  • Bo Thomsen
  • Christian Bendixen
  • Olaf-Georg Issinger
  • Brigitte Boldyreff
Article

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 

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References

  1. 1.
    Pinna LA: Casein kinase 2: An ‘eminence grise’ in cellular regulation? Biochim Biophys Acta 1054: 267–284, 1990PubMedGoogle Scholar
  2. 2.
    Issinger OG: Casein kinases: Pleiotropic mediators of cellular regulation. Pharmac Ther 59: 1–30, 1993Google Scholar
  3. 3.
    Allende JE, Allende CC: Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation. FASEB J 9: 313–323, 1995PubMedGoogle Scholar
  4. 4.
    Prowald K, Fischer H, Issinger OG: Enhanced casein kinase II activity in human tumour cell cultures. FEBS Lett 175: 479–483, 1984Google Scholar
  5. 5.
    Münstermann U, Fritz G, Seitz G, Lu YP, Schneider HR, Issinger OG: Casein kinase II is elevated in solid human tumours and proliferating non-neoplastic tissue. Eur J Biochem 189: 251–257, 1990PubMedGoogle Scholar
  6. 6.
    Seldin DC, Leder P: Casein kinase II alpha transgene-induced murine lymphoma: Relation to theileriosis in cattle. Science 267: 894–897, 1995PubMedGoogle Scholar
  7. 7.
    Appel K, Wagner P, Boldyreff B, Issinger OG, Montenarh, M: Mapping of the interaction sites of the growth suppressor protein p53 with the regulatory beta-subunit of protein kinase CK2. Oncogene 11: 1971–1978, 1995PubMedGoogle Scholar
  8. 8.
    Meggio F, Pinna LA: Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosol. Eur J Biochem 145: 593–599, 1984PubMedGoogle Scholar
  9. 9.
    Grankowski N, Boldyreff B, Issinger OG: Isolation and characterization of recombinant human casein kinase II subunits α and β from bacteria. Eur J Biochem 198: 25–30, 1991PubMedGoogle Scholar
  10. 10.
    Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger OG, Pinna LA: The effect of polylysine on casein-kinase-2 activity is influenced by both the structure of the protein/peptide substrates and the subunit composition of the enzyme. Eur J Biochem 205: 939–945, 1992PubMedGoogle Scholar
  11. 11.
    Meggio F, Boldyreff B, Marin 0, Pinna LA, Issinger OG: Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur J Biochern 204: 293–297, 1992Google Scholar
  12. 12.
    Gietz RD, Graharn KC, Litchfield DW: Interaction between the subunits of casein kinase II. J Biol Chem 270: 13017–13021, 1995PubMedGoogle Scholar
  13. 13.
    Kusk M, Bendixen C, Duno M, Westergaard O, Thornsen B: Genetic dissection of intersubunit contacts within human protein kinase CK2. J Mol Biol 253: 703–711, 1995Google Scholar
  14. 14.
    Boldyreff B, Mietens U, Issinger OG: Structure of protein kinase CK2: Dimerization of the human β-subunit. FEBS Lett 379: 153–156, 1996PubMedGoogle Scholar
  15. 15.
    Kim M, Cha JY, Marshak DR, Nae YS: Interaction of the β subunit of casein kinase II with ribosomal protein L5. Biochem Biophys Res Commun 226: 180–186, 1996PubMedGoogle Scholar
  16. 16.
    Boldyreff B, Issinger OG: A-Raf kinase is a new interacting partner of protein kinase CK2β subunit. FEBS Lett 403: 197–199, 1997PubMedGoogle Scholar
  17. 17.
    Hagemann C, Kalmes A, Wixler V, Wixler L, Schuster T, Rapp UR: The regulatory subunit of protein kinase CK2 is a specific A-Raf activator. FEBS Lett 403: 200–202, 1997PubMedGoogle Scholar
  18. 18.
    Chen M, Li D, Krebs EG, Cooper JA: The casein kinase II β subunit binds to Mos and inhibits Mos activity. Mol Cell Biol 17: 1904–1912, 1997PubMedGoogle Scholar
  19. 19.
    Filhol O, Baudier J, Delphin C, Loue-Mackenbach P, Chambaz EM, Cochet C: Casein kinase II and the tumor suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation. J Biol Chem 267: 20577–20583, 1992PubMedGoogle Scholar
  20. 20.
    Bojanowski K, Filhol O, Cochet C, Chambaz EM, Larsen AK: DNA topoisomerase II and casein kinase II associate in a molecular complex that is catalytically active. J Biol Chem 268: 22920–22926, 1993PubMedGoogle Scholar
  21. 21.
    Li D, Meier UT, Dobrowolska G, Krebs EG: Specific interaction between casein kinase 2 and the nucleolar protein Nopp140. J Biol Chem 272: 3773–3779, 1997PubMedGoogle Scholar
  22. 22.
    Bendixen C, Gangloff S, Rothstein R: A yeast mating-selection-scheme for detection of protein-protein interactions. Nucleic Acids Res 22: 1778–1779, 1994PubMedGoogle Scholar
  23. 23.
    Bartel PL, Chien CT, Sternglanz R, Fields S: Using the two-hybrid system to detect protein-protein interactions. In: D.A. Hartley (ed). Cellular Interactions in Development: A practical approach. Oxford University Press, Oxford, pp 153–179Google Scholar
  24. 24.
    Feilotter HE, Hannon GJ, Ruddell CJ, Beach D: Construction of an improved host strain for two hybrid screening. Nucleic Acids Res 22: 1502–1503, 1994PubMedGoogle Scholar
  25. 25.
    Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struffi K: Current Protocols in Molecular Biology, volume 2, New York: John Wiley & Sons Inc, 1994Google Scholar
  26. 26.
    Kaiser P, Auer B: Rapid shuttle plasmid preparation from yeast cells by transfer to E. coli. Bio Techniques 14: 552, 1993Google Scholar
  27. 27.
    Del Sal G, Manfioletti G, Schneider C: The CTAB-DNA precipitation method: A common miniscale preparation of template DNA from phagemids, phages or plasmids suitable for sequencing. Bio Techniques 7: 514–519, 1989Google Scholar
  28. 28.
    Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M: Human rsk isoforms: cloning and characterization of tissue-specific expression. Am J Physiol 266: 351–359, 1994Google Scholar
  29. 29.
    Todd R, Mcbridge J, Tsuji T, Donoff RB, Nagai M, Chou MY, Chiang T, Wong DTW: Deleted in oral cancer (doc-1), a novel oral tumor suppressor gene. FASEB J 9: 1362–1370, 1995PubMedGoogle Scholar
  30. 30.
    Chu K, Niu XH, Williams LT: A Fas-associated protein factor, FAF 1, potentiates Fas-mediated apoptosis. Proc Nad Acad Sci USA 92: 11894–11898, 1995Google Scholar
  31. 31.
    Ma L, Spremulli LL: Cloning and sequence analysis of the human mitochondrial translational initiation factor 2 cDNA. J Biol Chem 270: 1859–1865, 1995PubMedGoogle Scholar
  32. 32.
    Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: Exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet 92: 397–402, 1993PubMedGoogle Scholar
  33. 33.
    Krehan A, Lorenz P, Plana-Coll M, Pyerin W: Interaction sites between catalytic and regulatory subunits in human protein kinase CK2 holoenzyme as indicated by chemical cross linking and immunological investigations. Biochemistry 35: 4966–4975, 1996PubMedGoogle Scholar
  34. 34.
    Litchfield DW, Slominski E, Lewenza S, Narvey M, Bosc DG, Gietz RD: Analysis of interactions between the subunits of protein kinase CK2. Biochem Cell Biol 74: 541–547, 1996PubMedGoogle Scholar
  35. 35.
    Boldyreff B, Meggio F, Issinger OG, Pinna LA: Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated β-subunits. Biochemistry 32: 12672–12677, 1993PubMedGoogle Scholar
  36. 36.
    Marin O, Meggio F, Sarno S, Pinna LA: Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2β subunit. Biochemistry 36: 7192–7198, 1997PubMedGoogle Scholar
  37. 37.
    Boldyreff B, Meggio F, Pinna LA, Issinger OG: Efficient autophosphorylation and phosphorylation of the β-subunit by casein kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site. J Biol Chem 269: 4827–4831, 1994PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Mette Kusk
    • 1
  • Rehana Ahmed
    • 1
  • Bo Thomsen
    • 2
  • Christian Bendixen
    • 2
  • Olaf-Georg Issinger
    • 1
  • Brigitte Boldyreff
    • 1
  1. 1.Biokemisk InstitutOdense UniversitetOdenseDenmark
  2. 2.The Danish Institute of Animal SciencesResearch Center FoulumTjeleDenmark

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