Skip to main content

Distinctive features of plant protein kinase CK2

  • Chapter

Part of the book series: Molecular and Cellular Biochemistry ((DMCB,volume 35))

Abstract

In plants, protein kinase CK2 is involved in different processes that control many aspects of metabolism and development. In mammals and yeast the enzyme is a heterotetramer composed of two types of subunits. During years the subunit composition of the maize protein kinase CK2 enzyme has been a source of controversy. We have recently characterized the maize holoenzyme subunits. Our results show that multiple catalytic and regulatory subunits are expressed in maize and are able to specifically interact with other α and β subunits suggesting a high level of heterogeneity in the typical heterotetrameric structure. Here, we summarize data available on plant CK2 enzymes, in order to clarify the distinctive features and functions of plant protein kinase CK2. (Mol Cell Biochem 227: 119-127, 2001)

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

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Seldin DC, Leder P: Casein kinase II alpha transgene-induced murine lymphoma: Relation to theileriosis in cattle. Science 267: 894–896,1995

    Article  PubMed  CAS  Google Scholar 

  2. Löscher B, Kuenzel EA, Krebs EG, Eisenman RN: Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 8: 11111119, 1989

    Google Scholar 

  3. Hanna D, Rethinaswamy A, Glover CVC: Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J Biol Chem 270: 25905–25914, 1995

    Article  PubMed  CAS  Google Scholar 

  4. Yan T-FJ, Tao M: Purification and characterization of a wheat germ protein kinase. J Biol Chem 257: 7037–7043, 1982

    PubMed  CAS  Google Scholar 

  5. Dobrowolska G, Meggio F, Marchiori F, Pinna LA: Specific determinants of maize casein kinase II-B are related but distinct from those of rat liver casein kinase-2. Biochem Biophys Act 1010: 274–277, 1989

    Article  CAS  Google Scholar 

  6. Klimczak LJ, Schindler U, Cashmore AR: DNA binding activity of the Arabidopsis G-box binding factor GBFI is stimulated by phosphorylation by casein kinase H from broccoli. Plant Cell 4: 87–98, 1992

    PubMed  CAS  Google Scholar 

  7. Li H, Roux SJ: Casein kinase II protein kinase is bound to lamina-matrix and phosphorylates lamina-like protein in isolated pea nuclei. Proc Natl Acad Sci USA 89: 8434–8438, 1992

    Article  PubMed  CAS  Google Scholar 

  8. Dobrowolska G, Boldyreff B, Issinger O-G: Cloning and sequencing of the casein kinase 2 a subunit from Zea mays. Biochem Biophys Acta 1129: 139–140, 1991

    Article  PubMed  CAS  Google Scholar 

  9. Mizoguchi T, Yamaguchi-Shinozaki K, Hayashida N, Kamada H Shinozaki K: Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in Arabidopsis thaliana. Plant Mol Biol 21: 279–289, 1993

    Article  PubMed  CAS  Google Scholar 

  10. Collinge MA, Walker JC: Isolation of an Arabidopsis thaliana casein kinase II 13 subunit by complementation in Saccharomyces cerevisiae. Plant Mol Biol 25: 649–658, 1994

    CAS  Google Scholar 

  11. Sugano S, Andronis C, Green RM, Wang Z-Y, Tobin EM: Protein kinase CK2 interacts with and phosphorylates the Arabidopsis circadian clock-associated 1 protein. Proc Natl Acad Sci USA 95: 11020–11025,1998

    Article  PubMed  CAS  Google Scholar 

  12. Niefind K, Guerra B, Pinna LA, Issinger O-G, Schomburg D: Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. EMBO J 17: 2451–2462, 1998

    Article  PubMed  CAS  Google Scholar 

  13. Riera M, Peracchia G, de Nadal E, Ariño J, Pagès M: Maize protein kinase CK2: Regulation and functionality of three ß regulatory subunits. Plant J 25: 2001 (in press)

    Google Scholar 

  14. Lee Y, Lloyd AM, Roux SJ: Antisense expression of the CK2 alpha-subunit gene in Arabidopsis. Effects on light-regulated gene expression and plant growth. Plant Physiol 119: 989–1000, 1999

    Article  PubMed  CAS  Google Scholar 

  15. Espunya MC, Combettes B, Dot J, Chaubet-Gigot N, Martinez MC: Cell-cycle modulation of CK2 activity in tobacco BY-2 cells. Plant J 19: 655–666, 1999

    Article  PubMed  CAS  Google Scholar 

  16. Litchfield DW, Lozemann FJ, Piening C, Sommercorn J, Takio K, Walsch KA, Krebs, EG: Subunit structure of casein kinase II from bovine testis. J Biol Chem 265: 7638–7644, 1990

    PubMed  CAS  Google Scholar 

  17. Padmanabha R, Chen-Wu JLP, Hanna DE, Glover CVC: Isolation, sequencing, and disruption of the CKA2 gene: Casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol Cell Biol 10: 4089–4099, 1990

    CAS  Google Scholar 

  18. Peracchia G, Jensen AB, Culiáñez-Macià FA, Grosset J, Goday A, Issinger O-G, Pages M: Characterization, subcellular localization and nuclear targeting of casein kinase II from Zea mays. Plant Mol Biol 40: 199–211, 1999

    Article  PubMed  CAS  Google Scholar 

  19. Guerra B, Boldyreff B, Sarno S, Cesaro L, Issinger O-G, Pinna LA: CK2: A protein kinase in need of control. Pharmacol Ther 82: 303–313, 1999

    Article  PubMed  CAS  Google Scholar 

  20. Niefind K, Putter M, Guerra B, Issinger O-G, Schomburg D: GTP plus water mimic ATP in the active site of protein kinase CK2. Nat Struct Biol 6: 1100–1103, 1999

    Article  PubMed  CAS  Google Scholar 

  21. Battistutta R, Sarno S, De Moliner E, Marin O, Issinger O-G, Zanotti G, Pinna LA: The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme. Eur J Biochem 267: 5184–5190, 2000

    Article  PubMed  CAS  Google Scholar 

  22. Livak KJ: Detailed structure of the Drosophila melanogaster stellate genes and their transcripts. Genetics 124: 303–316, 1990

    PubMed  CAS  Google Scholar 

  23. Grankowski N, Boldyreff B, Issinger O-G: Isolation and characterization of recombinant human casein kinase H subunits a and f3 from bacteria. Eur J Biochem 198: 25–30, 1991

    Article  PubMed  CAS  Google Scholar 

  24. Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger O-G, Pinna LA: Role of 13 subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur J Biochem 204: 293–297, 1992

    Article  PubMed  CAS  Google Scholar 

  25. Bidwai AP, Reed JC, Glover CVC: Phosphorylation of calmodulin by the catalytic subunit of casein kinase II is inhibited by the regulatory subunit. Arch Biochem Biophys 300: 265–270, 1993

    Article  PubMed  CAS  Google Scholar 

  26. Bidwai AP, Reed JC, Glover CVC: Casein kinase II of Saccharomyces cerevisiae contains two distinct regulatory subunits, 13 and 13’. Arch Biochem Biophys 309: 348–355, 1994

    Article  PubMed  CAS  Google Scholar 

  27. Saxena A, Padmanabha R, Glover CVC: Isolation and sequencing of cDNA clones encoding the alpha and beta subunits of drosophila casein kinase II. Mol Cell Biol 7: 3409–3417, 1987

    PubMed  CAS  Google Scholar 

  28. Bidwai AP, Zhao W, Glover CVC: A gene located at 56F1–2 in Drosophila melanogaster encodes a novel metazoan beta-like subunit of casein kinase II. Mol Cell Biol Res Commun 1: 21–28, 1999

    Article  PubMed  CAS  Google Scholar 

  29. Bidwai AP, Reed JC, Glover CVC: Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharo- myces cerevisiae casein kinase II (CKII). Deletion of CKII regu-latory subunits elicits a salt-sensitive phenotype. J Biol Chem 270: 10395–10404, 1995

    Article  PubMed  CAS  Google Scholar 

  30. Dobrowolska G, Meggio F, Szczegielniak J, Muszynska G, Pinna LA: Purification and characterization of maize seedling casein kinase IIB, a monomeric enzyme immunologically related to the a subunit of animal casein kinase-2. Eur J Biochem 204: 299–303, 1992

    Article  Google Scholar 

  31. Boldyreff B, Meggio F, Dobrowolska G, Pinna LA, Issinger OG: Expression and characterization of a recombinant maize CK-2 a subunit. Biochim Biophys Acta 1173: 32–38, 1993

    Article  PubMed  CAS  Google Scholar 

  32. Chantalat L, Leroy D, Filhol O, Nueda A, Benitez MJ, Chambaz EM, Cochet C, Dideberg O: Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization. EMBO J 18: 2930–2940, 1999

    Article  PubMed  CAS  Google Scholar 

  33. Reed JC, Bidwai AP, Glover CVC: Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta’-subunit of Saccharomyces cerevisiae casein kinase II. J Biol Chem 269: 18192–18200, 1994

    PubMed  CAS  Google Scholar 

  34. Krehan A, Lorenz P, Plana-Coll M, Pyerin W: Interaction sites between catalytic and regulatory subunits in human protein kinase CK2 holoenzymes as indicated by chemical cross-linking and immunological investigations. Biochemistry 35: 4966–4975, 1996

    Article  PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  36. Litchfield DW, Lozeman FJ, Cicirelli MF, Harrylock M, Ericsson LH, Piening CJ, Krebs EG: Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2. J Biol Chem 266: 20380–20389, 1991

    PubMed  CAS  Google Scholar 

  37. Lin W-J, Sheu G-T, Traugh JA: Effects of autophosphorylation on casein kinase II activity: Evidence from mutations in the (3 subunit. Biochemistry 33: 6998–7004, 1994

    Article  PubMed  CAS  Google Scholar 

  38. Klimczak LJ, Collinge MA, Farini D, Giuliano G, Walker JC, Cashmore AR: Reconstitution of Arabidopsis casein kinase II from recombinant subunits and phosphorylation of transcription factor GBF1. Plant Cell 7: 105–115, 1995

    PubMed  CAS  Google Scholar 

  39. Guerra B, Issinger O-G: Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20: 2391–406, 1999

    Article  Google Scholar 

  40. Datta N, Cashmore AR: Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation. Plant Cell 1: 1069–1077, 1989

    PubMed  CAS  Google Scholar 

  41. Tjaden G, Coruzzi GM: A novel AT-rich DNA binding protein that combines an HMG-like DNA binding protein with a putative transcription domain. Plant Cell 6: 107–118, 1994

    PubMed  CAS  Google Scholar 

  42. Sugano S, Andronis C, Ong MS, Green, Tobin EM: The protein kinase CK2 is involved in regulation of circadian rhythms in Arabidopsis. Proc Natl Acad Sci USA 96: 12362–123626, 1999

    Google Scholar 

  43. Löscher B, Christenson E, Litchfield D, Krebs EG, Eisenman RN: Myb DNA binding inhibited by phosphorylation at site deleted during oncogenic activation. Nature 344: 517–521, 1990

    Article  Google Scholar 

  44. Hardtke CS, Gohda K, Osterlund MT, Oyama T, Okada K, Deng XW: HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain. EMBO J 19: 4997–5006, 2000

    Article  PubMed  CAS  Google Scholar 

  45. Ciceri P, Gianazza E, Lazzari B, Lippoli G, Genga A, Hoschek G, Schmidt RJ, Viotti A: Phosphorylation of Opaque 2 changes diurnally and impacts its DNA binding activity. Plant Cell 9: 97–108, 1997

    PubMed  CAS  Google Scholar 

  46. Ralet MC, Fouques D, Leonil J, Molle D, Meunier JC: Soybean beta-conglicin alpha subunit is phosphorylated on two distinct serines by protein kinase CK2 in vitro. J Protein Chem 18: 315323, 1999

    Google Scholar 

  47. Baldan B, Navazio L, Friso A, Mariani P, Meggio F: Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2. Biochem Biophys Res Commun 221: 498–502, 1996

    Article  PubMed  CAS  Google Scholar 

  48. Ou WJ, Thomas DY, Bell AW, Bergeron JJ: Protein casein kinase II phosphorylation of signal sequence receptor alpha and the associated membrane chaperone calnexin. J Biol Chem 267: 2378923796, 1992

    Google Scholar 

  49. Bailey-Serres J, Vangala S, Szick K, Lee CH: Acidic phosphoprotein complex of the 60S ribosomal subunit of maize seedling roots. Components and changes in response to flooding. Plant Physiol 114: 1293–305, 1997

    Article  PubMed  CAS  Google Scholar 

  50. Hasler P, Brot N, Weissbach H, Parnassa AP, Elkon K: Ribosomal proteins P0, P1 and P2 are phosphorylated by casein kinase II at their conserved carboxy termini. J Biol Chem 266: 13815–13820, 1991

    PubMed  CAS  Google Scholar 

  51. Kanekatsu M, Munakata H, Furuzono K, Ohtsuki K: Biochemical characterization of a 34 kDa ribonucleoprotein (p34) purified from the spinach chloroplast fraction as an effective phosphate acceptor for casein kinase II. FEBS Lett 335: 176–180, 1993

    Article  PubMed  CAS  Google Scholar 

  52. Janaki N, Krishna VM, Ramaiah KV: Phosphorylation of wheat germ initiation factor 2 (eIF-2) by N-ethylmaleimide-treated wheat germ lysates and by purified casein kinase II does not affect the guanine nucleotide exchange on eIF-2. Arch Biochem Biophys 324: 1–8, 1995

    Article  PubMed  CAS  Google Scholar 

  53. Pain VM, Clemens MJ: Assembly and breakdown of mammalian protein synthesis initiation complexes: Regulation by guanine nucleotides and by phosphorylation of initiation factor eIF-2. Biochemistry 22: 726–733, 1983

    Article  PubMed  CAS  Google Scholar 

  54. Tuteja N, Beven AF, Shaw PJ, Tuteja R: A pea homologue of human DNA helicase I is localized within the dense fibrillar component of the nucleolus and stimulated by phosphorylation with CK2 and cdc2 protein kinases. Plant J 25: 9–17, 2001

    Article  PubMed  CAS  Google Scholar 

  55. Plana M, Itarte E, Eritja R, Goday A, Pages M, Martinez MC: Phosphorylation of Maize RAB-17 protein by casein kinase 2. J Biol Chem 266: 22510–22514, 1991

    PubMed  CAS  Google Scholar 

  56. Goday A, Jensen AB, Culiañez-Macià FB, Albà MM, Figueras M, Serratosa J, Torrent M, Pages M: The maize abscisic acid-responsive protein rab17 is located in the nucleus and interacts with nuclear localization signals. Plant Cell 6: 351–360, 1994

    PubMed  CAS  Google Scholar 

  57. Jensen AB, Goday A, Figueras M, Jessop AC, Pages M: Phosphorylation mediates the nuclear targeting of the maize Rabl7 protein. Plant J 13: 691–697, 1998

    Article  PubMed  CAS  Google Scholar 

  58. Gerber DA, Souquere-Besse S, Puvion F, Dubois MF, Bensaude O, Cochet C: Heat-induced relocalization of protein kinase CK2. Implication of CK2 in the context of cellular stress. J Biol Chem 275: 23919–23926, 2000

    Article  PubMed  CAS  Google Scholar 

  59. Godoy JA, Lunar R, Torres-Schumann S, Moreno J, Rodrigo RM, Pintor-Toro JA: Expression, tissue distribution and subcellular localization of dehydrin TAS 14 in salt-stressed tomato plants. Plant Mol Biol 26: 1921–1934, 1994

    Article  PubMed  CAS  Google Scholar 

  60. Kanekatsu M, Saito H, Motohashi K, Hisabori T: The beta subunit of chloroplast ATP synthase (CFOCF1-ATPase) is phosphorylated by casein kinase II. Biochem Mol Biol Int 46: 99105, 1998

    Google Scholar 

  61. Hsieh HL, Song CJ, Roux SJ: Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II. Biochim Biophys Acta 1494: 248–255, 2000

    Article  PubMed  CAS  Google Scholar 

  62. Ohtsuki K, Nakamura S, Shimoyama Y, Shibata D, Munakata H, Yoshiki Y, Okubo K: A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. J Biochem (Tokyo) 118: 11451150, 1995

    Google Scholar 

  63. Umeda M, Manabe Y, Uchimiya H: Phosphorylation of the C2 subunit of the proteasome in rice (Oryza sativa L.). FEBS Lett 403: 313–317, 1997

    Article  PubMed  CAS  Google Scholar 

  64. Hidalgo P, Garreton V, Berrios CG, Ojeda H, Jordana X, Holuigue L: A nuclear casein kinase 2 activity is involved in early events of transcriptional activation induced by salicylic acid in tobacco. Plant Physiol 125: 396–405, 2001

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Springer Science+Business Media New York

About this chapter

Cite this chapter

Riera, M., Peracchia, G., Pagès, M. (2001). Distinctive features of plant protein kinase CK2. In: Ahmed, K., Issinger, OG., Allende, J.E. (eds) Protein Kinase CK2 — From Structure to Regulation. Molecular and Cellular Biochemistry, vol 35. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1723-8_15

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-1723-8_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5696-7

  • Online ISBN: 978-1-4615-1723-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics