Distinctive features of plant protein kinase CK2

Seldin DC, Leder P: Casein kinase II alpha transgene-induced murine lymphoma: Relation to theileriosis in cattle. Science 267: 894–896, 1995 Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN: Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 8: 1111–1119, 1989 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 Yan T-FJ, Tao M: Purification and characterization of a wheat germ protein kinase. J Biol Chem 257: 7037–7043, 1982 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 Klimczak LJ, Schindler U, Cashmore AR: DNA binding activity of the Arabidopsis G-box binding factor GBF1 is stimulated by phosphorylation by casein kinase II from broccoli. Plant Cell 4: 87–98, 1992 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 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 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 Collinge MA, Walker JC: Isolation of an Arabidopsis thaliana casein kinase II β subunit by complementation in Saccharomyces cerevisiae. Plant Mol Biol 25: 649–658, 1994 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 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 Riera M, Peracchia G, de Nadal E, Ariño J, Pagès M: Maize protein kinase CK2: Regulation and functionality of three β regulatory subunits. Plant J 25: 2001 (in press) 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 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 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 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 Peracchia G, Jensen AB, Culiáñez-Macià FA, Grosset J, Goday A, Issinger O-G, Pagès M: Characterization, subcellular localization and nuclear targeting of casein kinase II from Zea mays. Plant Mol Biol 40: 199–211, 1999 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 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 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 Livak KJ: Detailed structure of the Drosophila melanogaster stellate genes and their transcripts. Genetics 124: 303–316, 1990 Grankowski N, Boldyreff B, Issinger O-G: Isolation and characterization of recombinant human casein kinase II subunits α and β from bacteria. Eur J Biochem 198: 25–30, 1991 Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger O-G, Pinna LA: Role of β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur J Biochem 204: 293–297, 1992 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 Bidwai AP, Reed JC, Glover CVC: Casein kinase II of Saccharomyces cerevisiae contains two distinct regulatory subunits, β and β'. Arch Biochem Biophys 309: 348–355, 1994 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 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 Bidwai AP, Reed JC, Glover CVC: Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII regulatory subunits elicits a salt-sensitive phenotype. J Biol Chem 270: 10395–10404, 1995 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 Boldyreff B, Meggio F, Dobrowolska G, Pinna LA, Issinger OG: Expression and characterization of a recombinant maize CK-2 α subunit. Biochim Biophys Acta 1173: 32–38, 1993 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 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 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 Allende JE, and Allende CC: Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation. FASEB J 9: 313–323, 1995 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 Lin W-J, Sheu G-T, Traugh JA: Effects of autophosphorylation on casein kinase II activity: Evidence from mutations in the β subunit. Biochemistry 33: 6998–7004, 1994 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 Guerra B, Issinger O-G: Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20: 2391–406, 1999 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 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 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 Lüscher 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 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 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 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: 315–323, 1999 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 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: 23789–23796, 1992 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 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 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 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 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 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 Plana M, Itarte E, Eritja R, Goday A, Pagès M, Martinez MC: Phosphorylation of Maize RAB-17 protein by casein kinase 2. J Biol Chem 266: 22510–22514, 1991 Goday A, Jensen AB, Culiañez-Macià FB, Albà MM, Figueras M, Serratosa J, Torrent M, Pagès 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 Jensen AB, Goday A, Figueras M, Jessop AC, Pagès M: Phosphorylation mediates the nuclear targeting of the maize Rab17 protein. Plant J 13: 691–697, 1998 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 Godoy JA, Lunar R, Torres-Schumann S, Moreno J, Rodrigo RM, Pintor-Toro JA: Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants. Plant Mol Biol 26: 1921–1934, 1994 Kanekatsu M, Saito H, Motohashi K, Hisabori T: The beta subunit of chloroplast ATP synthase (CF0CF1-ATPase) is phosphorylated by casein kinase II. Biochem Mol Biol Int 46: 99–105, 1998 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 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: 1145–1150, 1995 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 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