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The genomic structure of two protein kinase CK2α genes of Xenopus laevis and features of the putative promoter region

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Abstract

Protein kinase CK2 is an enzyme that is ubiquitous in eukaryotes. This enzyme, composed of catalytic (α and α′) and regulatory (β) subunits, is responsible for the phosphorylation of a large number of proteins and is implicated in cell division. Genomic clones coding for the CK2α subunit of Xenopus laevis have been isolated. Initial restriction enzyme profiles and subsequent PCR analysis and DNA sequencing indicated that these genomic clones correspond to two different genes. The two genes are highly homologous in the regions of the coding sequence (only 3 amino acid differences) but differ considerable in their intron sequences and lengths. Gene 1 corresponds to the cDNA of XlCK2α which had been previously isolated and described. The genomic clone for this gene was truncated. Gene 2 contains the entire coding region for CK2α subunit as well as a fragment of 6.4 kb of the 5'upstream region. The exon/intron boundries of both genes obey the GT/AG rule with the exception of intron V where the less common GC/AG is seen. Comparison of the size of ten coding exons and sites where these are interrupted by introns shows strong conservation with respect to the human CK2α gene. RT-PCR analysis of mRNAs from X. laevis ovary, oocytes and early embryos using a specific primer for gene 2 demonstrated that this gene is expressed in these tissues and cells. Analysis of transcription start sites using 5′RACE and RNA from stage VI oocytes demonstrated that there are multiple start sites in the XlCK2α mRNA. It was also seen that a noncoding exon 1 is present 4 kb upstream of the translation start site and that alternate splicing occurs in gene 2 to give exon 1 of different lengths. Sequencing of the entire upstream genomic region of gene 2 revealed that there are regions of homology to the sequence of exon 1 of the human CK2α gene. Other sequences with consensus to transcription factor binding sites that are seen in the promoter region of human CK2α are also found in the X. laevis CK2α gene 2. These sites include Ets1, E2F, CCAAT and GC rich regions. No canonical TATA motif is observed.

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References

  1. Allende JE, Allende CC: Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulations. FASEB J 9: 313–323, 1995

    Google Scholar 

  2. Pinna LA, Meggio F: Protein kinase CK2 and its implication in cell division and proliferation. Prog Cell Cycle Res 3: 77–97, 1997

    Google Scholar 

  3. Guerra B, Issinger OG: Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20: 391–408, 1999

    Google Scholar 

  4. Seldin DC, Leder P: Casein kinase II alpha is a novel lymphoid oncogene in a mouse model of tropical theileriosis of cattle. Science 267: 894–897, 1995

    Google Scholar 

  5. Ole-MoiYoi OK, Brown WC, Iams KP, Nayar A, Tsukamoto T, Mackin 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, 1993

    Google Scholar 

  6. Voss H, Wirkner U, Jakobi R, Hewitt NA, Schwager C, Wimmermann J, Ansorge W, Pyerin W: Structure of the gene encoding human casein kinase II subunit β. J Biol Chem 266: 13706–13711, 1991

    Google Scholar 

  7. Wirkner U, Voss H, Ansorge W, Pyerin W: Genomic organization and promoter identification of the human protein kinase CK2 catalytic subunit α (CSNK2A1). Genomics 48: 71–78, 1998

    Google Scholar 

  8. Krehan A, Ansuini H, Bocher O, Grein W, Wirkner U, Pyerin W: Transcription factors Ets1, MF-κB, and Sp1 are major determinants of the promoter activity of the human protein kinase CK2α gene. J Biol Chem 275: 18327–18336, 2000

    Google Scholar 

  9. Gustincich S, Manfioloetti G, Del Sal G, Schneider C, Carnici P: A fast method for high quality genomic DNA extraction from whole blood. Biotechniques 11: 298–302, 1991

    Google Scholar 

  10. Jedlicki A, Hinrichs MV, Allende CC, Allende JE: The cDNAS coding for the α and β subunits of Xenopus laevis casein kinase II. FEBS Lett 297: 280–284, 1992

    Google Scholar 

  11. Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidimium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156–159, 1987

    Google Scholar 

  12. Wilhelm V, Rojas P, Gatica M, Allende CC, Allende JE: Expression of the subunits of protein kinase CK2 during oogenesis in Xenopus laevis. Eur J Biochem 232: 671–676, 1995

    Google Scholar 

  13. Xu X, Toselli PA, Russell LD, Seldin DC: Globozoospermia in mice lacking the casein kinase II alpha′ catalytic subunit. Nat Genet 23: 118–121, 1999

    Google Scholar 

  14. Plant KE, Hair A, Morgan GT: Genes encoding isoforms of transcription elongation factor TFIIS in Xenopus and the use of multiple unusual RNA processing signals. Nucleic Acids Res 24: 3514–3521, 1996

    Google Scholar 

  15. 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. Biochim Biophys Acta 1131: 220–222, 1992

    Google Scholar 

  16. Hanks SK, Hunter T: The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification. FASEB J 9: 576–596, 1995

    Google Scholar 

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Correspondence to Catherine C. Allende.

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Wilhelm, V., Neckelman, G., Allende, J.E. et al. The genomic structure of two protein kinase CK2α genes of Xenopus laevis and features of the putative promoter region. Mol Cell Biochem 227, 175–183 (2001). https://doi.org/10.1023/A:1013173109643

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  • DOI: https://doi.org/10.1023/A:1013173109643

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