Skip to main content
SpringerLink
Log in

Proteins of theXenopus laevis zinc finger multigene family as targets for CK II phosphorylation

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Zn finger proteins (ZFPs) of the C2/H2 type inXenopus laevis are encoded by a multigene family comprising several hundred members. Based upon conserved sequence features outside the Zn finger region, ZFPs can be subdivided into distinct subfamilies. Two of such subfamilies are characterized by conserved, N-terminal amino acid sequences termed the FAX and the FAR Domain. Here we present data suggesting that the zinc finger proteins of the FAR-ZFP subfamily are targets for CK II mediated phosphorylation. Expression of these proteins during oogenesis coincides with CK II activity in unfertilized eggs. Additionally, we have found that XIcOF 7.1, a member of the FAX-ZFP subfamily, is also phosphorylated by CK II. The target sites forin vitro phosphorylation are localized within the conserved N-terminal domains but not within the Zn finger regions. However, amino acid sequence comparison revealed that individual phosphoacceptor sites are not generally conserved among all members of the respective ZFP subfamilies. The relevance of a potential CK II phosphorylation for the regulation of ZFP activityin vivo is discussed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Köster M, Pieler T, Pöting, A and Knöchel W: The finger motif defines a multigene family represented in the maternal mRNA of Xenopus laevis oocytes. EMBO J. 7: 1735–1741, 1988

    Google Scholar 

  2. Nietfeld W, El-Baradi T, Mentzel H, Pieler T, Köster M, Pöting, A and Knöchel, W.: Second-order repeats inXenopus laevis finger proteins. J Mol Biol 208: 639–659, 1989

    Google Scholar 

  3. Bellefroid EJ, Lecocq PJ, Benhida A, Poncelet DA, Belayew A and Martial JA: The human genome contains hundreds of genes coding for finger proteins of the Krüppel type. DNA 8: 377–387, 1989

    Google Scholar 

  4. El-Baradi T and Pieler T: Zinc finger proteins: What we know and what we would like to know. Mech Dev 35: 155–169, 1991

    Google Scholar 

  5. Schuh R, Aicher W, Gaul U, Coté S, Preiss A, Maier D, Seifert E, Nauber U, Schröder C, Kemler, R and Jäckle H: A conserved family of nuclear proteins containing structural elements of the finger protein encoded by Krüppel, aDrosophila segmentation gene. Cell 47: 1025–1032, 1986

    Google Scholar 

  6. Bellefroid EJ, Poncelet DA, Lecocq PJ, Reveland O and Martial JA: The evolutionarily conserved Krüppel-associated box domain defines a subfamily of eukaryotic multifingered proteins. Proc Natl Acad Sci USA 88: 3608–3612, 1991

    Google Scholar 

  7. Rosati M, Marino M, Franze A, Tramontano A and Grimaldi G: Members of the zinc finger protein gene family sharing a conserved N-terminal module. Nucl Acids Res 19: 5661–5667, 1991

    Google Scholar 

  8. Knöchel W, Pöting A, Köster M, El-Baradi T, Nietfeld W, Bouwmeester T and Pieler T: Evolutionary conserved modules associated with zinc fingers in Xenopus, laevis. Proc Natl Acad Sci USA 86: 6097–6100, 1989

    Google Scholar 

  9. Klocke B, Köster M, Hille S, Bouwmeester T, Böhm, S, Pieler T and Knöchel W: The FAR Domain a newXenopus laevis zinc finger protein subfamily with specific poly(U) homopolymer binding activity. Biochim Biophys Acta 1217: 81–89, 1994

    Google Scholar 

  10. El-Baradi T, Bouwmeester T, Giltay R and Pieler T: The maternal store of zinc finger protein encoding mRNAs in fully grownXenopus oocytes is not required for early embryogenesis. EMBO J 10: 1407–1413, 1991

    Google Scholar 

  11. Nietfeld W, Conrad S, van Wijk I, Giltay R, Bouwmeester T, Knöchel W and Pieler T: Evidence for a clustered genomic organization of FAX-zinc finger protein encoding transcription units inXenopus laevis. J Mol Biol 230: 400–412, 1993

    Google Scholar 

  12. can Wijk I, Burfeind J and Pieler T: Nuclear transport and phosphorylation of the RNA bindingXenopus zinc finger protein XFG 5-1. Mech Dev 39: 63–72, 1992

    Google Scholar 

  13. Köster M, Kühn U, Bouwmeester T, Nietfeld W, El-Baradi T, Knöchel W and Pieler T: Structure, expression andin vitro functional characterization of a novel RNA binding zinc finger protein fromXenopus. EMBO J 10: 3087–3093, 1991

    Google Scholar 

  14. Pinna LA: Casein kinase 2 an ‘eminence grise’ in cellular regulation? Biochim Biophys Acta 1054: 267–284, 1990

    Google Scholar 

  15. Nietfeld W, Mentzel H and Pieler T: TheXenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains. EMBO J 9: 3699–3705, 1990

    Google Scholar 

  16. Harlow E and Lane D: Antibodies: A laboratory manual. Cold spring harbor laboratory press, 1988

  17. Kuenzel EA and Krebs EG: A synthetic peptide substrate specific for casein kinase II. Proc Natl Acad Sci USA 82: 737–741, 1985

    Google Scholar 

  18. Kenally PJ and Krebs EG: Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266: 15555–15558, 1989

    Google Scholar 

  19. Maridor G, Krek W and Nigg EA: Structure and expression of chicken nucleolin and NO38: Coordinate expression of two abundant nonribosomal nucleolar proteins. Biochem Biophys Acta 1049: 126–133, 1990

    Google Scholar 

  20. Litchfield DW, Lozeman FJ, Cicirelli MF, Harrylock M, Ericsson LH, Piening CJ and Krebs EG: Phosphorylation of the b subunit of casein kinase II in human A431 cells. J Biol Chem 266: 20380–29389, 1991

    Google Scholar 

  21. Ollo R and Maniatis, T:Drosophila Krüppel gene product in a baculovirus expression system is a nuclear phosphoprotein that binds DNA. Proc Natl Acad Sci 84: 5700–5704, 1987

    Google Scholar 

  22. Jackson SP, MacDonald JJ, Lees-Miller S and Tjian R: GC box binding induces phophorylation of Sp 1 by a DNA dependent protein kinase. Cell 63: 155–165, 1990

    Google Scholar 

  23. Krek W, Maridor G and Nigg EA: Casein kinase II is a predominantly nuclear enzyme. J Cell Biol 116: 43–55, 1992

    Google Scholar 

  24. Stigare J, Buddelmeijer N, Pigon A and Egyhazi E: A majority of casein kinase II a subunit is tightly bound to intranuclear components but not to b subunit. Mol Cell Biochem 129: 77–85, 1993

    Google Scholar 

  25. Voit R, Schnapp A, Kuhn A, Rosenbauer H, Hirschmann P, Stunnenberg HG and Grummt, I: The nucleolar transcription mUBF is phos-phorylated by casein kinase II in the C-terminal hyperacidic tail which is essential for transactivation. EMBO J 11: 2211–2218, 1992

    Google Scholar 

  26. Lin A, Frost J, Deng T, Smeal T, Al-Alawi N Kikkawa U, Hunter T, Brenner D and Karin M: Casein Kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity. Cell 70: 777–789, 1992

    Google Scholar 

  27. Marais RM, Hsuan JJ, McGuigan C, Wynne J and Treisman R: Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. EMBO J 11: 97–105, 1992

    Google Scholar 

  28. Blackwood EM, Lüscher B and Eisenman RN: Myc and Max associatein vivo. Genes Dev 6: 71–80, 1992

    Google Scholar 

  29. Berberich SJ and Cole MD: Casein kinase II inhibits the DNA binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev 6: 166–176, 1992

    Google Scholar 

  30. Holcomb ER and Friedman DL: Phosphorylation of the C-proteins of HeLa cell hnRNP particles. J Biol Chem 259: 31–40, 1984

    Google Scholar 

  31. Friedman DL, Kleiman NJ and Campbell, FE: Nuclear phosphorylation in isolated nuclei from HeLa cells. Evidence that32P incorporation from [g-32P] GTP is catalyzed by nuclear kinase II. Biochim Biophys Acta 857: 165–176, 1985

    Google Scholar 

  32. Mayrand SH, Dwen P and Pederson T: Serine/threonine phosphorylation regulates binding of C hnRNP proteins to pre-mRNA. Proc Natl Acad Sci 90: 7764–7768, 1993

    Google Scholar 

  33. Mulner-Lorillon O, Cormier P, Labbée, J-C, Dorée M, Pouhle R, Osborne H and Bellé R: M-phase specific edc2 protein kinase phosphorylates the b subunit of casein kinase II and increases casein kinase II activity. Eur J Biochem 193: 529–534, 1990

    Google Scholar 

  34. Litchfield DW, Lüscher B, Lozeman FJ, Eisenman RN and Krebs EG: Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis. J Biol Chem 267: 13943–13951, 1992

    Google Scholar 

  35. Litchfield DW and Lüscher B: Casein Kinase II in signal transduction and cell cycle regulation. Mol Cell Biochem 127/128: 187–199, 1993

    Google Scholar 

  36. Rogers S, Wells R and Rechsteiner M: Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234: 364–368, 1986

    Google Scholar 

  37. Rechsteriner M, Rogers S and Rote K: Protein structure and intracellular stability. Trends in Biochem Sci 12: 390–394, 1987

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Abt. Biochemie, Univeristät Ulm, Albert Einstein Allee 11, 89081, Ulm, Germany

    Bernward Klocke & Walter Knöchel

Authors
  1. Bernward Klocke
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Walter Knöchel
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Klocke, B., Knöchel, W. Proteins of theXenopus laevis zinc finger multigene family as targets for CK II phosphorylation. Mol Cell Biochem 142, 49–59 (1995). https://doi.org/10.1007/BF00928913

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00928913

Key words

Search

Navigation