Isolation of an Arabidopsis thaliana casein kinase II β subunit by complementation in Saccharomyces cerevisiae
Received: 20 January 1994 Accepted: 01 April 1994 DOI:
Cite this article as: Collinge, M.A. & Walker, J.C. Plant Mol Biol (1994) 25: 649. doi:10.1007/BF00029603 Abstract
Casein kinase II is thought to play an essential role in the control of cell division and differentiation in all eukaryotes. Through complementation of a defective casein kinase II catalytic subunit gene from
Saccharomyces cerevisiae, we isolated an Arabidopsis thaliana casein kinase II regulatory subunit homologue, CKB1. A second regulatory subunit was identified by low-stringency hybridization with CKB1.
Casein kinase II from
S. cerevisiae is composed of two catalytic (α) and two regulatory (β) subunits. Simultaneous disruption of the genes for the α and α′ subunits, CKA1 and CKA2, respectively, is lethal. Strain YDH8 has disruptions of CKA1 and CKA2; its viability depends on a temperature-sensitive allele of CKA2, cka2–8, carried on a centromeric plasmid. We screened an A. thaliana cDNA library, whose inserts are under the control of the galactose-inducible GAL10 promoter, for cDNAs which enabled YDH8 cells to grow at the restrictive temperature. One cDNA, CKB1, was isolated by this screen which had homology to cDNAs of casein kinase II β subunits. A second cDNA, CKB2, was isolated by hybridization and was also able to suppress the YDH8 mutant phenotype.
The proteins encoded by
CKB1 and CKB2 are 80% identical. The carboxy-terminal two thirds of both proteins is ca. 54% identical to the regulatory β subunits of casein kinase II from other species. The amino termini are unrelated to any other known proteins. CKB1 and CKB2 lack the conserved autophosphorylation site characteristic of animal β subunits, but have potential casein kinase II phosphorylation sites in the same region. Suppression of the cka1 Δ cka2–8 mutant phenotype occurs by interaction of CKB1 with the defective, cka2–8-encoded, catalytic subunit. Cells with disruptions in CKA1 and CKA2 are not rescued by expression of CKB1. Key words cDNA regulatory subunit plant protein kinase yeast References
Bidwai AP, Hanna DE, Glover CVC: Purification and characterization of casein kinase II (CKII) from Δcka1 Δ
cka2 Saccharomyces cerevisiae
CKII subunits. J Biol Chem 267: 18790–18796 (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: Subunit composition of casein kinase II from
: evidence that the yeast enzyme contains two distinct regulatory beta subunits. J Cell Biochem (S17A): 274–274 (1993).
Boldyreff B, Meggio F, Dobrowolska G, Pinna LA, Issinger O-G: Expression and characterization of a recombinant maize CK-2 α subunit. Biochim Biophys Acta 1173: 32–38 (1993).
Boldyreff B, Meggio F, Pinna LA, Issinger O-G: Casein kinase-2 structure-function relationship: creation of a set of mutants of the β subunit that variably surrogate the wild type β subunit function. Biochem Biophys Res Comm 188: 228–234 (1992).
Boldyreff B, Meggio F, Pinna LA, Issinger O-G: Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated β-subunits. Biochemistry 32: 12672–12677 (1993).
Boldyreff B, Piontek K, Schmidt-Spaniol I, Issinger O-G: The β subunit of casein kinase II: cloning of cDNAs from murine and porcine orgin and expression of the porcine sequence as a fusion protein. Biochim Biophys Acta 1088: 439–441 (1991).
Chen-Wu J, Padmanabha R, Glover CVC: Isolation, sequencing, and disruption of the
gene encoding the alpha subunit of yeast casein kinase II. Mol Cell Biol 8: 4981–4990 (1988).
Dobrowolska G, Boldryeff B, Issinger O-G: Cloning and sequencing of the casein kinase 2 α subunit from
. Biochim Biophys Acta 1129: 139–140 (1991).
Dobrowolska G, Meggio F, Pinna LA: Characterization of multiple forms of maize seedling protein kinases reminiscent of animal casein kinases S (type 1) and TS (type 2). Biochim Biophys Acta 931: 188–195 (1987).
Dobrowolska G, Meggio F, Szczegielnaik J, Muszynska G, Pinna LA. Purification and characterization of maize seedling casein kinase IIB, a monomeric enzyme immunologically related to the α subunit of animal casein kinase-2. Eur J Biochem 204: 299–303 (1992).
Dower WJ, Miller JF, Ragsdale CW: High efficiency transformation of
by high voltage electroporation. Nucl Acids Res 16: 6127–6145 (1988).
Elble R. A simple and efficient procedure for transformation of yeasts. Bio Techniques 13: 18–20 (1992).
Gaber RF, Culbertson MR. Frameshift suppression in
. IV. New suppressors among spontaneous co-revertants of the group II
frameshift mutations. Genetics 101: 345–367 (1982).
Gowda S, Pillay DTN: Cyclic AMP independent protein kinases from soybean cotyledons (
L.). Plant Sci Lett 25: 49–59 (1982).
Haffner MH, Chin MB, Lane BG: Wheat embryo ribonucleates. XII. Formal characterization of terminal and penultimate nucleoside residues at the 5′ ends of capped RNA from imbibing wheat embryos. Can J Biochem 56: 729–733 (1978).
Hoffman CS, Winston F: A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of
. Gene 57: 267–272 (1987).
Hu E, Rubin CS: Casein kinase II from
: cloning, characterization, and developmental regulation of the gene encoding the β subunit. J Biol Chem 266: 19796–19802 (1991).
Jakobi R, Voss H, Pyerin W: Human phosvitin/casein kinase type II. Eur J Biochem 183: 227–233 (1989).
Jedlicki A, Hinrichs MV, Allende CC, Allende JE: The cDNAs coding for the α- and β-subunits of
casein kinase II. FEBS Lett 297: 280–284 (1992).
Johnston M, Davis RW: Sequences that regulate the divergent
. Mol Cell Biol 4: 1440–1448 (1984).
Kassir Y, Simchen G. Monitoring meiosis and sporulation in
. Meth Enzymol 194: 94–110 (1991).
Klimczak LJ, Schindler U, Cashmore AR: DNA binding activity of the
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 lamin-like protein in isolated pea nuclei. Proc Natl Acad Sci USA 89: 8434–8438 (1992).
Li H, Roux SJ: Purification and characterization of casein kinase 2-type protein kinase from pea nuclei. Plant Physiol 99: 686–692 (1992).
Lin W-J, Tuazon PT, Traugh JA: Characterization of the catalytic subunit of casein kinase II expressed in
and regulation of activity. J Biol Chem 266: 5664–5669 (1991).
Litchfield SW, Lozeman FJ, Cicirelli MF, Harrylock M, Ericsson LH, Piening CJ, Krebs EG. Phosphorylation of the β subunit of casein kinase II in human A431 cells. J Biol Chem 266: 20380–20389 (1991).
Livak KJ: Detailed structure of the
Drosophila melanogaster stellate
genes and their transcripts. Genetics 124: 303–316 (1990).
Meggio F, Boldryeff B, Issinger O-G, Pinna LA: The autophosphorylation and p34
2 phosphorylation sites of casein kinase-2 β-subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme. Biochim Biophys Acta 1164: 223–225 (1993).
Meggio F, Boldryeff B, Marin O, Pinna LA, Issinger O-G: Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted enzyme. Eur J Biochem 204: 293–297 (1992).
Mizoguchi T, Yamaguchi-Shinozaki K, Hayashida N, Kamada H, Shinozaki K: Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in
. Plant Mol Biol 21: 279–289 (1993).
Padmanabha R, Chen-Wu J, Hanna DE, Glover CVC: Isolation, sequencing, and disruption of the yeast
gene: casein kinase II is essential for viability in
. Mol Cell Biol 10: 489–4099 (1990).
Padmanabha R, Glover CVC: Casein kinase II of yeast contains two distinct α polypeptides and an unusually large β subunit. J Biol Chem 262: 1829–1835 (1987).
Pinna LA: Casein kinase 2: an ‘eminence grise’ in cellular regulation? Biochim Biophys Acta 1054: 267–284 (1990).
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).
Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).
Sanger F, Miklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 4: 5463–5467 (1977).
Saxena A, Padmanabha R, Glover CVC: Isolation and sequencing of cDNA clones encoding alpha and beta subunits of
casein kinase II. Mol Cell Biol 7: 3409–3417 (1987).
Schiestl RH, Gietz RD: High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genet 16: 339–346 (1989).
Short JM, Fernandez JM, Sorge JA, Huse WD: λZAP: A bacteriophage λ expression vector with
excision properties. Nucl Acids Res 16: 7583 (1988).
Sikorski R, Hieter P: A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in
. Genetics 122: 19–27 (1989).
Smith RD, Walker JC: Expression of multiple type I phosphoprotein phosphatases in
Plant Mol Biol 21: 307–316 (1993).
Tuazon PT, Traugh JA: Casein kinase I and II—multipotential serine protein kinases: structure, function and regulation. In: Greengard P, Robinson GA (eds) Advances in Second Messenger and Phosphoprotein Research, pp. 123–164. Raven Press, New York (1991).
Yan T-FJ, Tao M: Purification and characterization of wheat germ protein kinase. J Biol Chem 257: 7037–7043 (1982).
Zhang S, Jin C-D, Roux SJ: Casein kinase II-type protein kinase from pea cytoplasm and its inactivation by alkaline phospahtase
. Plant Physiol 103: 955–962 (1993).
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