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Volumn 156, Issue 4, 2000, Pages 492-503

Separation and purification of both CK-I and CK-II casein kinases in developing maize endosperm - Phosphorylation of native HMG proteins

Author keywords

Casein kinases; Enzyme characterization; Enzyme purification; Phosphorylation of native proteins; Zea mays L.

Indexed keywords

ZEA MAYS;

EID: 0034082572     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0176-1617(00)80164-9     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 0018085511 scopus 로고
    • Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay
    • Bearden, J. C.: Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay. Biochim. Biophys. Acta 533, 525-529 (1978).
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 525-529
    • Bearden, J.C.1
  • 2
    • 0342463407 scopus 로고
    • The nucleus
    • Bonner, J., and J. E. Varuer (eds.): Academic Press, New York
    • Bonner, J.: The nucleus. In: Bonner, J., and J. E. Varuer (eds.): Plant Biochemistry, pp. 38-40. Academic Press, New York (1976).
    • (1976) Plant Biochemistry , pp. 38-40
    • Bonner, J.1
  • 3
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Hunter, T., and B. M. Sefton (eds.): Academic Press Inc., San Diego, California
    • Boyle, W. J., P. van der Geer and T. Hunter: Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. In: Hunter, T., and B. M. Sefton (eds.): Methods in Enzymology, Vol. 201, Protein Phosphorylation, pp. 110-149. Academic Press Inc., San Diego, California (1991).
    • (1991) Methods in Enzymology, Vol. 201, Protein Phosphorylation , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 4
    • 0027962833 scopus 로고
    • Nuclear casein-kinase II type activity in pea root tip cells during germination
    • Brusa, P., L. Nannariello and E. Sparvoli: Nuclear casein-kinase II type activity in pea root tip cells during germination. Plant Science 102, 31-40 (1994).
    • (1994) Plant Science , vol.102 , pp. 31-40
    • Brusa, P.1    Nannariello, L.2    Sparvoli, E.3
  • 5
    • 0000308241 scopus 로고
    • Regulation of enzyme activity in plants by reversible phosphorylation
    • Budde, R. J. A., and R. Chollet: Regulation of enzyme activity in plants by reversible phosphorylation. Physiol. Plant. 72, 435-439 (1988).
    • (1988) Physiol. Plant. , vol.72 , pp. 435-439
    • Budde, R.J.A.1    Chollet, R.2
  • 6
    • 0026567876 scopus 로고
    • Purification and characterization of maize seedling casein kinase IIB, a monomeric enzyme immunologically related to a subunit of animal casein kinase-2
    • Dobrowolska, G., 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 a subunit of animal casein kinase-2. Eur. J. Biochem. 204, 299-303 (1992).
    • (1992) Eur. J. Biochem. , vol.204 , pp. 299-303
    • Dobrowolska, G.1    Meggio, F.2    Szczegielniak, J.3    Muszynska, G.4    Pinna, L.A.5
  • 7
    • 0000781495 scopus 로고
    • Characterization of multiple forms of maize seedling kinases reminiscent of animal casein kinases S (type 1) and TS (type 2)
    • Dobrowolska, G., F. Meggio and L. A. Pinna: Characterization of multiple forms of maize seedling kinases reminiscent of animal casein kinases S (type 1) and TS (type 2) Biochim. Biophys. Acta 931, 188-195 (1987).
    • (1987) Biochim. Biophys. Acta , vol.931 , pp. 188-195
    • Dobrowolska, G.1    Meggio, F.2    Pinna, L.A.3
  • 8
    • 0021969964 scopus 로고
    • The intracellular distribution and function of the high mobility group chromosomal proteins
    • Einck, L., and M. Bustin: The intracellular distribution and function of the high mobility group chromosomal proteins. Exp. Cell Res. 156, 295-310 (1985).
    • (1985) Exp. Cell Res. , vol.156 , pp. 295-310
    • Einck, L.1    Bustin, M.2
  • 9
    • 0020490237 scopus 로고
    • Two proteins from nuclei of cultured tobacco cells with properties similar to the cyclic nucleotide-independent enzymes (NI and NII) from animal tissue
    • Erdmann, H., M. Bocher and K. G. Wagner: Two proteins from nuclei of cultured tobacco cells with properties similar to the cyclic nucleotide-independent enzymes (NI and NII) from animal tissue. FEBS Lett. 137, 245-248 (1982).
    • (1982) FEBS Lett. , vol.137 , pp. 245-248
    • Erdmann, H.1    Bocher, M.2    Wagner, K.G.3
  • 10
    • 0024311611 scopus 로고
    • A nuclear casein type II kinase from maize endosperm phosphorylating HMG proteins
    • Grasser, K. D., U. G. Maier and G. Feix: A nuclear casein type II kinase from maize endosperm phosphorylating HMG proteins. Biochem. Biophys. Res. Commun. 162, 456-463 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 456-463
    • Grasser, K.D.1    Maier, U.G.2    Feix, G.3
  • 11
    • 0025219024 scopus 로고
    • Maize high mobility group proteins bind to CCAAT and TATA boxes of a zein gene promoter
    • Grasser, K. D., U. G. Maier, M. M. Haass and G. Feix: Maize high mobility group proteins bind to CCAAT and TATA boxes of a zein gene promoter. J. Biol. Chem. 265, 4185-4188 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 4185-4188
    • Grasser, K.D.1    Maier, U.G.2    Haass, M.M.3    Feix, G.4
  • 12
    • 0026777153 scopus 로고
    • Oligomeric structure and autophosphorylation of nucleoside diphosphate kinase from rat mucosal mast cells
    • Hemmerich, S., and I. Pecht: Oligomeric structure and autophosphorylation of nucleoside diphosphate kinase from rat mucosal mast cells. Biochemistry 31, 4580-4587 (1992).
    • (1992) Biochemistry , vol.31 , pp. 4580-4587
    • Hemmerich, S.1    Pecht, I.2
  • 13
    • 0023651349 scopus 로고
    • A thousand and one protein kinases
    • Hunter, T.: A thousand and one protein kinases. Cell 50, 823-829 (1987).
    • (1987) Cell , vol.50 , pp. 823-829
    • Hunter, T.1
  • 15
    • 0001684349 scopus 로고
    • Biochemical characterization of casein kinase II (CK-II) from cultured cells of the liverwort, Marchantia polymorpha
    • Kanekatsu, M., and K. Ohtsuki: Biochemical characterization of casein kinase II (CK-II) from cultured cells of the liverwort, Marchantia polymorpha. Plant Cell Physiol. 34, 627-631 (1993).
    • (1993) Plant Cell Physiol. , vol.34 , pp. 627-631
    • Kanekatsu, M.1    Ohtsuki, K.2
  • 16
    • 0028834157 scopus 로고
    • Properties and specificity of a calcium dependent endonuclease from germinated lentil (Lens culinaris)
    • Kefalas, P. S., and T. Yupsanis: Properties and specificity of a calcium dependent endonuclease from germinated lentil (Lens culinaris). J. Plant Physiol. 146, 1-9 (1995).
    • (1995) J. Plant Physiol. , vol.146 , pp. 1-9
    • Kefalas, P.S.1    Yupsanis, T.2
  • 17
    • 0026480127 scopus 로고
    • DNA binding activity of the Arabidopsis G-box binding factor GBF1 is stimulated by phosphorylation by casein kinase II from broccoli
    • Klimczak, L. J., U. Schindler and A. R. Cashmore: 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).
    • (1992) Plant Cell , vol.4 , pp. 87-98
    • Klimczak, L.J.1    Schindler, U.2    Cashmore, A.R.3
  • 18
    • 0027296086 scopus 로고
    • Purification and characterization of casein kinase I from broccoli
    • Klimczak, L. J., and A. R. Cashmore: Purification and characterization of casein kinase I from broccoli. Biochem. J. 293, 283-288 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 283-288
    • Klimczak, L.J.1    Cashmore, A.R.2
  • 19
    • 0029137355 scopus 로고
    • Reconstitution of Arabidopsis casein kinase II from recombinant subunits and phosphorylation of transcription factor GBF 1
    • Klimczak, L. J., 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 GBF 1. Plant Cell 7, 105-115 (1995).
    • (1995) Plant Cell , vol.7 , pp. 105-115
    • Klimczak, L.J.1    Collinge, M.A.2    Farini, D.3    Giuliano, G.4    Walker, J.C.5    Cashmore, A.R.6
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0027765725 scopus 로고
    • Protein kinase inhibitors in plants of the Myrtaceae, Proteaceae, and Leguminosae
    • Larkin, M., J. Brazier, B. Ternai and G. M. Polya: Protein kinase inhibitors in plants of the Myrtaceae, Proteaceae, and Leguminosae. Planta Med. 59, 485-578 (1993).
    • (1993) Planta Med. , vol.59 , pp. 485-578
    • Larkin, M.1    Brazier, J.2    Ternai, B.3    Polya, G.M.4
  • 23
    • 0026884030 scopus 로고
    • Purification and characterization of a casein 2-type protein kinase from pea nuclei
    • Li, H., and S. J. Roux: Purification and characterization of a casein 2-type protein kinase from pea nuclei. Plant Physiol. 99, 686-692 (1992).
    • (1992) Plant Physiol. , vol.99 , pp. 686-692
    • Li, H.1    Roux, S.J.2
  • 24
    • 0020491268 scopus 로고
    • Protein kinases from spinach chloroplasts. II. Protein substrate specificity and kinetic properties
    • Lucero, H. A., Z. F. Lin and E. Racker: Protein kinases from spinach chloroplasts. II. Protein substrate specificity and kinetic properties. J. Biol. Chem. 257, 12157-12160 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 12157-12160
    • Lucero, H.A.1    Lin, Z.F.2    Racker, E.3
  • 25
    • 0031260188 scopus 로고    scopus 로고
    • Purification and characterization of a protein kinase from winged bean
    • Mukhopadhyay, K.: Purification and characterization of a protein kinase from winged bean. Phytochemistry 46, 461-467 (1997).
    • (1997) Phytochemistry , vol.46 , pp. 461-467
    • Mukhopadhyay, K.1
  • 27
    • 0006190003 scopus 로고
    • Isolation and characterization of a chromatin-associated protein kinase from soybean
    • Murray, M. G., T. J. Guilfoyle and J. L. Key: Isolation and characterization of a chromatin-associated protein kinase from soybean. Plant Physiol. 61, 1023-1030 (1978a).
    • (1978) Plant Physiol. , vol.61 , pp. 1023-1030
    • Murray, M.G.1    Guilfoyle, T.J.2    Key, J.L.3
  • 28
    • 0006158045 scopus 로고
    • Isolation and preliminary characterization of a casein kinase from cauliflower nuclei
    • _ _ _ Isolation and preliminary characterization of a casein kinase from cauliflower nuclei. Plant Physiol. 62, 434-437 (1978b).
    • (1978) Plant Physiol. , vol.62 , pp. 434-437
  • 29
    • 0342897510 scopus 로고
    • Polypeptides from maize seedlings with protein kinase functions
    • Muszynska, G., G. Dobrowolska and E. Ber: Polypeptides from maize seedlings with protein kinase functions. Biochim. Biophis. Acta 757, 316-323 (1983).
    • (1983) Biochim. Biophis. Acta , vol.757 , pp. 316-323
    • Muszynska, G.1    Dobrowolska, G.2    Ber, E.3
  • 30
    • 0023664669 scopus 로고
    • Protein kinase C autophosphorylation by an intrapeptide reaction
    • Newton, A. C., and D. E. Koshland Jr.: Protein kinase C autophosphorylation by an intrapeptide reaction. J. Biol. Chem. 262, 10185-10188 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 10185-10188
    • Newton, A.C.1    Koshland D.E., Jr.2
  • 31
    • 0025113220 scopus 로고
    • Casein kinase 2: An «eminence grise» in cellular regulation?
    • Pinna, L. A.: Casein kinase 2: an «eminence grise» in cellular regulation? Biochim. Biophis, Acta 1054, 267-284 (1990).
    • (1990) Biochim. Biophis, Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 32
    • 0001806586 scopus 로고
    • Phosphorylation of proteins in plants: Regulatory effects and potential involvement in stimulus/ response coupling
    • Ranjeva, R., and A. M. Boudet: Phosphorylation of proteins in plants: Regulatory effects and potential involvement in stimulus/ response coupling. Annu. Rev. Plant Physiol. 38, 73-93 (1987).
    • (1987) Annu. Rev. Plant Physiol. , vol.38 , pp. 73-93
    • Ranjeva, R.1    Boudet, A.M.2
  • 33
    • 0015217626 scopus 로고
    • Purification and properties of rabbit skeletal muscle adenosine 3′,5′-monophosphate-dependent protein kinases
    • Reimann, E. M., D. A. Walsh and E. G. Krebs: Purification and properties of rabbit skeletal muscle adenosine 3′,5′-monophosphate-dependent protein kinases. J. Biol. Chem. 246, 1986-1995 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 1986-1995
    • Reimann, E.M.1    Walsh, D.A.2    Krebs, E.G.3
  • 34
    • 0017273131 scopus 로고
    • Determination of proteolytic activities on casein substrates
    • Lorand, L. (ed.): Academic Press, New York
    • Reimerdes, E. H., and H. Klostermeyer: Determination of proteolytic activities on casein substrates. In: Lorand, L. (ed.): Methods Enzymol., Vol. XLV, Proteolytic Enzymes part B, pp. 26-28. Academic Press, New York (1976).
    • (1976) Methods Enzymol., Vol. XLV, Proteolytic Enzymes Part B , vol.45 , pp. 26-28
    • Reimerdes, E.H.1    Klostermeyer, H.2
  • 35
    • 0019015092 scopus 로고
    • Purification and characterisation of adenosine-3′,5′-phosphate-independent protein kinase from wheat germ
    • Rychlik, W., and W. Zagorski: Purification and characterisation of adenosine-3′,5′-phosphate-independent protein kinase from wheat germ. Eur. J. Biochem. 106, 653-659 (1980).
    • (1980) Eur. J. Biochem. , vol.106 , pp. 653-659
    • Rychlik, W.1    Zagorski, W.2
  • 36
    • 0028836318 scopus 로고
    • Purification and partial characterization of an acidic ribosomal protein kinase from maize
    • Sepulveda, G., R. Aguilar and E. Sanchez de Jimenez: Purification and partial characterization of an acidic ribosomal protein kinase from maize. Physiol. Plant. 94, 715-772 (1995).
    • (1995) Physiol. Plant. , vol.94 , pp. 715-772
    • Sepulveda, G.1    Aguilar, R.2    Sanchez De Jimenez, E.3
  • 37
    • 0017104546 scopus 로고
    • A polyethylene glycol/dextran procedure for the isolation of chromatin proteins (histones and non histones) from wheat germ
    • Simon, J. H., and W. M. Becker: A polyethylene glycol/dextran procedure for the isolation of chromatin proteins (histones and non histones) from wheat germ. Biochim. Biophys. Acta 454, 154-171 (1976).
    • (1976) Biochim. Biophys. Acta , vol.454 , pp. 154-171
    • Simon, J.H.1    Becker, W.M.2
  • 38
    • 0021759738 scopus 로고
    • High-mobility group chromosomal proteins of wheat
    • Spiker, S.: High-mobility group chromosomal proteins of wheat. J. Biol. Chem. 259, 12007-12013 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 12007-12013
    • Spiker, S.1
  • 39
    • 2742542982 scopus 로고
    • DNase I sensitivity of transcriptionally active genes in intact nuclei and isolated chromatin of plants
    • Spiker, S., M. G. Murray and W. F. Thompson: DNase I sensitivity of transcriptionally active genes in intact nuclei and isolated chromatin of plants. Proc. Natl. Acad. Sci. USA 80, 815-819 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 815-819
    • Spiker, S.1    Murray, M.G.2    Thompson, W.F.3
  • 40
    • 0029310678 scopus 로고
    • Plant protein kinase families and signal transduction
    • Stone, J. M., and J. C. Walker: Plant protein kinase families and signal transduction. Plant Physiol. 108, 451-457 (1995).
    • (1995) Plant Physiol. , vol.108 , pp. 451-457
    • Stone, J.M.1    Walker, J.C.2
  • 41
    • 0005021360 scopus 로고
    • Post-translational modification of proteins by phosphorylation
    • Trewavas, A.: Post-translational modification of proteins by phosphorylation. Annu. Rev. Plant Plysiol. 27, 349-374 (1976).
    • (1976) Annu. Rev. Plant Plysiol. , vol.27 , pp. 349-374
    • Trewavas, A.1
  • 42
    • 0026039891 scopus 로고
    • Casein kinase I and II-multipotential serine protein kinases: Structure, function, and regulation
    • Greengard, P., and G. A. Robinson (eds.): Raven Press, Ltd., New York
    • Tuazon, P. T., and J. A. Traugh: Casein kinase I and II-multipotential serine protein kinases: structure, function, and regulation. In: Greengard, P., and G. A. Robinson (eds.): Advances in Second Messenger and Phosphoprotein Research, pp. 123-164. Raven Press, Ltd., New York (1991).
    • (1991) Advances in Second Messenger and Phosphoprotein Research , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 43
    • 0021816430 scopus 로고
    • Phosphorylation of high mobility group protein 14 by casein kinase II
    • Walton, G. M., J. Spiess and G. N. Gill: Phosphorylation of high mobility group protein 14 by casein kinase II. J. Biol. Chem. 260, 4745-4750 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 4745-4750
    • Walton, G.M.1    Spiess, J.2    Gill, G.N.3
  • 44
    • 0020490737 scopus 로고
    • Purification and characterization of a wheat germ protein kinase
    • Yan, T.-F. J., and M. Tao: Purification and characterization of a wheat germ protein kinase. J. Biol. Chem. 257, 7037-7043 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 7037-7043
    • Yan, T.-F.J.1    Tao, M.2
  • 45
    • 0001879917 scopus 로고
    • Chromatin-associated nucleases of germinating barley
    • Yupsanis, T., and J. G. Georgatsos: Chromatin-associated nucleases of germinating barley. Int. J. Biochem. 15, 959-963 (1983).
    • (1983) Int. J. Biochem. , vol.15 , pp. 959-963
    • Yupsanis, T.1    Georgatsos, J.G.2
  • 46
    • 38249024083 scopus 로고
    • A heat-stable Mg-independent protein kinase of germinated barley seed
    • Yupsanis, T., A. Hadjiangelou and J. G. Georgatsos: A heat-stable Mg-independent protein kinase of germinated barley seed. Phytochemistry 28, 385-388 (1989).
    • (1989) Phytochemistry , vol.28 , pp. 385-388
    • Yupsanis, T.1    Hadjiangelou, A.2    Georgatsos, J.G.3
  • 47
    • 0002437524 scopus 로고
    • Seed protein electrophoresis for varietal identification in rice (Oryza sativa L.)
    • Yupsanis, T., M. Moustakas and S. Karakoli: Seed protein electrophoresis for varietal identification in rice (Oryza sativa L.). J. Agron. Crop Science 168, 95-99 (1992).
    • (1992) J. Agron. Crop Science , vol.168 , pp. 95-99
    • Yupsanis, T.1    Moustakas, M.2    Karakoli, S.3
  • 48
    • 0000602837 scopus 로고
    • Multiplicity of metal-independent protein phosphatases of germinated alfalfa seeds
    • Yupsanis, T., P. Eleftetiou, A. Pantazaki and J. G. Georgatsos: Multiplicity of metal-independent protein phosphatases of germinated alfalfa seeds. J. Plant Physiol. 141, 257-262 (1993).
    • (1993) J. Plant Physiol. , vol.141 , pp. 257-262
    • Yupsanis, T.1    Eleftetiou, P.2    Pantazaki, A.3    Georgatsos, J.G.4
  • 49
    • 84989078114 scopus 로고
    • Protein phosphorylation and protein patterns in developing endosperms of barley
    • Yupsanis, T., and P. R. Shewry: Protein phosphorylation and protein patterns in developing endosperms of barley. Plant Breeding 111, 73-77 (1993).
    • (1993) Plant Breeding , vol.111 , pp. 73-77
    • Yupsanis, T.1    Shewry, P.R.2
  • 50
    • 0027133386 scopus 로고
    • Casein kinase II-type protein kinase from pea cytoplasm and its inactivation by alkaline phosphatase in vitro
    • Zhang, S., 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, 955-962 (1993).
    • (1993) Plant Physiol. , vol.103 , pp. 955-962
    • Zhang, S.1    Jin, C.D.2    Roux, S.J.3


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