CK2α loci in the human genome: Structure and transcriptional activity

  • Ute Wirkner
  • Walter Pyerin
Part of the Developments in Molecular and Cellular Biochemistry book series (DMCB, volume 27)


Two CK2α loci are present in the human genome. First, locus 20p13, that contains the CK2α coding gene. It spans around 70 kb, is composed of 13 exons and shows homology to the respective gene in the nematode Caenorhabditis elegans. The translation start site is located in the second exon, the stop codon in exon 13. Two transcription start sites were identified, the further 5′ located site defines position 1 of the gene, the second site is located at position 50, respectively. The promoter region shows characteristics of a so-called house keeping gene: A high GC content, lack of aTATA-box and presence of several GC-boxes. By reporter gene assays, the promoter region of the CK2α gene could be located between position −256 and 144 relative to the first transcription start site. In the 3′ noncoding region of the CK2α gene, six polyadenylation signals were identified. As indicated by Northern blot analysis and by comparison with expressed sequence tags from the EMBL databank, the most 3′ located, active polyadenylation signal seems to be the fourth defining the end of the CK2α gene. The second CK2α locus is at 11p15. It contains a processed pseudogene, which shows all typical features of a processed sequence, such as absence of introns, short poly-A tail and direct flanking repeats. Interestingly, it contains a complete open reading frame and has potential promoter elements in its 5′ region. Nevertheless, no promoter activity could be detected in reporter gene assays. (Mol Cell Biochem 191: 59–64, 1999)

Key words

protein kinase CK2 genes gene structure and organization gene promoter activation human 


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  1. 1.
    Pinna LA: Casein kinase 2: An ‘eminence grise’ in cellular regulation. Biochim Biophys Acta 1054: 267–284, 1990PubMedCrossRefGoogle Scholar
  2. 2.
    Tuazon PT, Traugh JA: Casein kinase I and II — multipotential serine protein kinases: Structure, function and regulation. Adv Sec Mess Phosphoprot Res 23: 123–163, 1991Google Scholar
  3. 3.
    Meek DW, Street AJ: Nuclear phosphorylation and growth control. Biochem J 287: 1–15, 1992PubMedGoogle Scholar
  4. 4.
    Pyerin W, Ackermann K, Lorenz P: Casein kinases. In: F. Marks (ed). Protein Phosphorylation. VHC Verlagsgesellschaft mBH, Weinheim Germany, 1996, pp 117–147CrossRefGoogle Scholar
  5. 5.
    Padmanabha R, Chen-Wu JL-W, Hanna DE, Glover CVC: Isolation, sequencing and distribution of yeast CKA2 gene: Casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol Cell Biol 10: 4089–4099, 1990PubMedGoogle Scholar
  6. 6.
    Issinger, O-G: Casein kinases: Pleiotropic mediators of cellular regulation. Pharmac Ther 59: 1–30, 1993CrossRefGoogle Scholar
  7. 7.
    Allende JE, Allende CC: Protein kinase CK2: An enzyme with multiple substrates and apuzzling regulation. FASEB J 9: 313–323, 1995PubMedGoogle Scholar
  8. 8.
    Pepperkok R, Lorenz P, Jakobi R, Ansorge W, Pyerin W: Cell growth stimulation by EGF: Inhibition through antisense-oligonucleotides demonstrates important role of casein kinase II. Exp Cell Res 197: 245–253, 1991PubMedCrossRefGoogle Scholar
  9. 9.
    Pepperkok R, Lorenz P, Ansorge W, Pyerin W: Casein kinase II is required for transition of G0/G1 early G1 and G1/S phases of the cell cycle. J Biol Chem 269: 6986–6991, 1994PubMedGoogle Scholar
  10. 10.
    Ulloa L, Diaz-Nido J, Avila J: Depletion of casein kinase II by antisense oligonucleotide prevents neurotogenesis in neuroblastoma cells. EMBO J 12: 1633–1640, 1993PubMedGoogle Scholar
  11. 11.
    Meisner H, Heller-Harrison R, Buxton J, Czech MP: Molecular cloning of the human casein kinase II α subunit. Biochemistry 28: 4072–4076, 1989PubMedCrossRefGoogle Scholar
  12. 12.
    Maridor G, Park W, Krek W, Nigg E: Casein kinase II: cDNA sequences, developmental expression, and tissue distribution of mRNAs for α, α′ and β subunits of the chicken enzyme. J Biol Chem 266: 2362–2368, 1991PubMedGoogle Scholar
  13. 13.
    Ole-MoiYoi OK, Brown WC, lams KP, Nayar A, Tsukamoto T, Macklin MD: Evidence for the induction of casein kinase II in bovine lymphocytes transformed by the intracellular protozoan parasite Theileria parva. EMBO J 12: 1621–1631, 1993PubMedGoogle Scholar
  14. 14.
    Seldin DC, Leder P: Casein kinase Ha transgene-induced murine lymphoma: relation to theileriosis in cattle. Science 267: 894–897, 1995PubMedCrossRefGoogle Scholar
  15. 15.
    Chen-Wu JLP, Padmanabha R, Glover CVC: Isolation, sequencing, and disruption of the CKA1 gene encoding the alpha subunit of yeast casein kinase II. Mol Cell Biol 8: 4981–990, 1988PubMedGoogle Scholar
  16. 16.
    Reed JC, Bidwai AP, Glover CVC: Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory β′-subunit ofSacharomyces cerevisiae casein kinase II. J Biol Chem 269: 18192–18200, 1994PubMedGoogle Scholar
  17. 17.
    Bidwai AP, Reed CJ, Glover CVC: Cloning and disruption of CKB1, the gene encoding the 38-kDa β subunit of Sacharomyces cerevisiae casein kinase II. J Biol Chem 270: 10395–10404, 1995PubMedCrossRefGoogle Scholar
  18. 18.
    Roussou I, Dreatta G: The Schizosacharomyces pombe casein kinase II a and β subunit: Evolutionary conservation and positive role of the β subunit. Mol Cell Biol 14: 576–586, 1994PubMedGoogle Scholar
  19. 19.
    Ole-MoiYoi OK, Sugimoto C, Conrad PA, Macklin MD: Cloning and characterization of the casein kinase II a subunit gene from the lymphocyte transforming intracellular protozoan parasite Theileria parva. Biochem 31: 6193–6202, 1992CrossRefGoogle Scholar
  20. 20.
    Hu E, Rubin CS: Casein kinase II from Caenorhabditis elegans. J Biol Chem265: 5072-5080, 1990Google Scholar
  21. 21.
    Hu E, Rubin CS: Casein kinase II from Caenorhabditis elegans. J Biol Chem 266: 19796–19802, 1991PubMedGoogle Scholar
  22. 22.
    Hoffmann U, Hecht R, Boldyreff B, Issinger O-G: Characterization of the cDNA and three processed pseudogenes from the murine protein kinase CK2 a subunit. Biochim Biophys Acta 1260: 337–340, 1995PubMedCrossRefGoogle Scholar
  23. 23.
    Boldyreff B, Issinger O-G: Structure of the gene encoding the murine protein kinase CK2β subunit. Genomics 29: 253–256, 1995PubMedCrossRefGoogle Scholar
  24. 24.
    Yang-Feng TL, Teitz T, Cheung MC, Kan YW, Canaani D: Assignment of the human casein kinase II β-subunit gene to 6p 12-p21. Genomics 8: 741–742, 1990PubMedCrossRefGoogle Scholar
  25. 25.
    Voss H, Wirkner U, Jaeobi R, Hewitt N, Schwager C, Zimmermann J, Ansorge W, Pyerin W: The structure of the gene encoding human casein kinase II subunit beta. J Biol Chem 266: 13706–13711, 1991PubMedGoogle Scholar
  26. 26.
    Yang-Feng TL, Naiman T, Kopatz I, Eli D, Dafni N, Canaani D: Assignment of the human casein kinase IIα′ subunit gene (CSNK2A1) to chromosome 16pl3.2-pl3.3. Genomics 19: 173, 1994PubMedCrossRefGoogle Scholar
  27. 27.
    Wirkner U, Voss H, Lichter P, Weitz S, Ansorge W, Pyerin W: Human casein kinase II subunit α: Sequence of a processed (pseudo)gene and its localization on chromosome 11. Biochem Biophys Acta 1131: 220–222, 1992PubMedCrossRefGoogle Scholar
  28. 28.
    Albertsen HM, Abderrahim H, Cann HM, Dausset J, Le Paslier D, Cohen D: Construction and characterization of a yeast artificial chromosome library containing seven haploid human genome equivalents. Proc Natl Acad Sci USA 87: 4256–4260, 1990PubMedCrossRefGoogle Scholar
  29. 29.
    Wirkner U, Voss H, Ansorge W, Pyerin W: Genomic organization and promoter identification of the human protein kinase CK2 catalytic subunit α. Genomics 48: 71–78, 1998PubMedCrossRefGoogle Scholar
  30. 30.
    Ansorge W, Sproat B, Stegemann J, Schwager C, Zenke W: Automated DNA sequencing: Ultrasensitive detection of fluorescent bands during electrophoresis. Nucl Acid Res 15: 4593–4602, 1987CrossRefGoogle Scholar
  31. 31.
    Wirkner U, Voss H, Lichter P, Ansorge W, Pyerin W: The human gene (CSNK2A1) coding for the casein kinase subunit α is located on chromosome 20 and contains tandemly arranged Alu repeats. Genomics 19: 257–265, 1994PubMedCrossRefGoogle Scholar
  32. 32.
    Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG: Isolation and characterisation of human cDNA clones encoding the α and the α′ subunit of casein kinase II. Biochemistry 29: 8436–8447, 1990PubMedCrossRefGoogle Scholar
  33. 33.
    Wahle E, Keller W: The biochemistry of 3′-end cleavage and polyadenylation of messenger RNA precursors. Annu Rev Biochem 61: 419–440, 1992PubMedCrossRefGoogle Scholar
  34. 34.
    Wirkner U, Voss H, Lichter P, Pyerin W: Human protein kinase CK2 genes. Cell Mol Biol Res 40: 489–499, 1994PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1999

Authors and Affiliations

  • Ute Wirkner
    • 1
  • Walter Pyerin
    • 1
  1. 1.Biochemische Zellphysiologie, Deutsches KrebsforschungszentrumHeidelbergGermany

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