Identification of two different molecular forms of Arabidopsis thaliana casein kinase II

Plant Science

Volumn 124, Issue 2, 1997, Pages 131-142

  Espunya, M Carme ^a   Martínez, M Carmen ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

Arabidopsis; Casein kinase II; Molecular isoforms; Plant kinases

Indexed keywords

CASEIN KINASE II;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME REGULATION; ENZYME STRUCTURE; NONHUMAN; PLANT; PROTEIN ISOLATION;

ARABIDOPSIS THALIANA;

EID: 0343488334     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(96)04599-2     Document Type: Article

References (28)

1. J.E. Allende and C.C. Allende, Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J., 9 (1995) 313-323.
2. A.P. Bidwai, J.C. Reed and C.V.C. Glover, Casein kinase II of Saccharomyces cerevisiae contains two distinct regulatory subunits, β and β′. Arch. Biochem. Biophys., 309 (1994) 348-355.
3. T.-F Yan and M. Tao, Purification and characterization of a wheat germ protein kinase. J. Biol. Chem., 257 (1982) 7037-7043.
4. H. Erdmann, M. Böcher and K.G. Wagner, Two protein kinases from nuclei of cultured cells with properties similar to the cyclic nucleotide-independent enzymes (NI and NII) from animal tissue. FEBS Lett., 137 (1982) 245-248.
5. G. Dobrowolska, F. Meggio, J. Szczegielniak, G. Muszynska and L.A. Pinna, 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 (1992) 299-303.
6. L.J. Klimczak and A.R. Cashmore, Microheterogeneous cytosolic high-mobility group proteins from broccoli copurify with and are phosphorylated by casein kinase II. Plant Physiol., 105 (1994) 911-919.
7. G. Dobrowolska, F. Meggio and L.A. Pinna, 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 (1987) 188-195.
8. S. Zhang, C.-D. Jin and S.J. Roux, Casein kinase II-type protein kinase from pea cytoplasm and its inactivation by alkaline phosphatase in vitro. Plant Physiol., 103 (1993) 955-962.
9. G. Dobrowolska, B. Boldyreff and O.-G. Issinger, Cloning and sequencing of the casein kinase 2 α subunit from Zea mays. Biochim. Biophys. Acta, 1129 (1991) 139-140.
10. T. Mizoguchi, K. Yamaguchi-Shinozaki, N. Hayashida, H. Kamada and K. Shinozaki, Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in Arabidopsis thaliana. Plant Mol. Biol., 21 (1993) 279-289.
11. M.A. Collinge and J.C. Walker, Isolation of an Arabidopsis thaliana casein kinase II β subunit by complementation in Saccharomyces cerevisiae. Plant Mol. Biol., 25 (1994) 649-658.
12. L.J. Klimczak, M.A. Collinge, D. Farini, G. Giuliano, J.C. Walker and A.R. Cashmore, Reconstitution of Arabidopsis casein kinase II from recombinant subunits and phosphorylation of transcription factor GBF1. Plant Cell, 7 (1995) 105-115.
13. T. Murashige and F. Skoog, A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant., 15 (1962) 473-497.
14. M. Plana, E. Itarte, R. Eritja, A. Goday, M. Pagès and M.C. Martinez, Phosphorylation of maize RAB-17 protein by casein kinase 2. J. Biol. Chem., 266 (1991) 22510-22514.
15. J.R. Leatherbarrow, Enzfitter: A Nonlinear Regression Data Analysis Program for the IBM-PC, Elsevier Biosoft, Cambridge, UK, 1987.
16. K.P. Huang and J.C. Robinson, A rapid and sensitive assay method for protein kinase. Anal. Biochem., 72 (1976) 593-599.
17. M.E. Dahmus, Purification and properties of calf thymus casein kinases I and II. J. Biol. Chem., 256 (1981) 11239-11243.
18. G.K. Dahmus, C.V.C. Glover, D.L. Brutlag and M.E. Dahmus, Similarities in structure and function of calf thymus and Drosophila casein kinase II. J. Biol. Chem., 259 (1984) 9001-9006.
19. A.P. Bidwai, D.E. Hanna and C.V.C. Glover, Purification and characterization of casein kinase II (CKII) from ckal cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo. J. Biol. Chem., 267 (1992) 18790-18796.
20. A.P. Bidwai, J.C. Reed and C.V.C. Glover, Phosphorylation of calmodulin by the catalytic subunit of casein kinase II is inhibited by the regulatory subunit. Arch. Biochem. Biophys., 300 (1993) 265-270.
21. E. Molina, M. Plana and E. Itarte, Heterogeneity of rat liver cytosol casein kinase 2. Biochem. J., 277 (1991) 811-818.
22. B. Boldyreff, F. Meggio, G. Dobrowolska, L.A. Pinna, and O.G. Issinger, Expression and characterization of a recombinant maize CK-2 χ subunit. Biochim. Biophys. Acta, 1173 (1993) 32-38.
23. G.M. Hathaway and J.A. Traugh, Casein kinase II. Methods Enzymol., 99 (1983) 317-331.
24. F. Meggio, B. Boldyreff, O. Marin, L.A. Pinna and O.-G. Issinger, Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur. J. Biochem., 204 (1992) 293-297.
25. F. Meggio, O. Marin and L.A. Pinna, Substrate specificity of protein kinase CK2. Cell. Mol. Biol. Res., 40 (1994) 401-409.
26. B. Boldyreff, F. Meggio, L.A. Pinna and O.-G. Issinger, Efficient autophosphorylation and phosphorylation of the ß -subunit by casein kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site. J. Biol. Chem., 269 (1994) 4827-4831.
27. M.V. Hinrichs, M. Gatica, C.C. Allende and J.E. Allende. Site-directed mutants of the ß subunit of protein kinase CK2 demonstrate the important role of Pro-58. FEBS Lett., 368 (1995) 211-214.
28. cdc2 phosphorylation sites of casein kinase-2 β-subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme. Biochim. Biophys. Acta, 1164 (1993) 223-225.