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Volumn 55, Issue 4, 2008, Pages 767-776

Catalytic activity of mutants of yeast protein kinase CK2α

Author keywords

ATP binding; ATP competitive inhibitors; Heparin; Mutagenesis; Protein kinase CK2; Protein phosphorylation; Saccharomyces cerevisiae; Spermine; Yeast

Indexed keywords

SACCHAROMYCES CEREVISIAE;

EID: 58249144669     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2008_3039     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 2442418622 scopus 로고    scopus 로고
    • Rapid site-directed mutagenesis using two-pcr-generated DNA fragments reproducing the plasmid template
    • Allemandou F, Nussberger J, Brunner HR, Brakch N (2003) Rapid site-directed mutagenesis using two-pcr-generated DNA fragments reproducing the plasmid template. J Biomed Biotechnol 2003: 202-207.
    • (2003) J Biomed Biotechnol , vol.2003 , pp. 202-207
    • Allemandou, F.1    Nussberger, J.2    Brunner, H.R.3    Brakch, N.4
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modeling
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modeling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 0033884005 scopus 로고    scopus 로고
    • 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
    • Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA (2000) 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) Eur J Biochem , vol.267 , pp. 5184-5190
    • Battistutta, R.1    Sarno, S.2    De Moliner, E.3    Marin, O.4    Issinger, O.G.5    Zanotti, G.6    Pinna, L.A.7
  • 4
    • 0034775155 scopus 로고    scopus 로고
    • Structural features underlying selective inhibition of protein kinase CK2 by ATP-site directed tetrabromo benzotriazole
    • Battistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA (2001) Structural features underlying selective inhibition of protein kinase CK2 by ATP-site directed tetrabromo benzotriazole. Protein Sci 10: 2200-2206.
    • (2001) Protein Sci , vol.10 , pp. 2200-2206
    • Battistutta, R.1    De Moliner, E.2    Sarno, S.3    Zanotti, G.4    Pinna, L.A.5
  • 6
    • 38349116517 scopus 로고    scopus 로고
    • Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2
    • Duncan JS, Litchfield DW (2008) Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2. Biochim Biophys Acta 1784: 33-47.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 33-47
    • Duncan, J.S.1    Litchfield, D.W.2
  • 7
    • 0033837291 scopus 로고    scopus 로고
    • Subcellular localization of protein kinase CK2. A key to its function?
    • Faust M, Montenarh M (2000) Subcellular localization of protein kinase CK2. A key to its function? Cell Tissue Res 301: 329-340.
    • (2000) Cell Tissue Res , vol.301 , pp. 329-340
    • Faust, M.1    Montenarh, M.2
  • 8
    • 0030021720 scopus 로고    scopus 로고
    • Elevated protein kinase CK2 activity in chromatin of head and neck tumors: association with malignant transformation
    • Faust AF, Gapany M, Tristani P, Davis A, Adams LA, Ahmed K (1996) Elevated protein kinase CK2 activity in chromatin of head and neck tumors: association with malignant transformation. Cancer Lett 101: 31-35.
    • (1996) Cancer Lett , vol.101 , pp. 31-35
    • Faust, A.F.1    Gapany, M.2    Tristani, P.3    Davis, A.4    Adams, L.A.5    Ahmed, K.6
  • 9
    • 2442594082 scopus 로고    scopus 로고
    • Protein kinase CK2: a new view of an old molecular complex
    • Filhol O, Martiel JL, Cochet C (2004) Protein kinase CK2: a new view of an old molecular complex. EMBO Rep 5: 351-355.
    • (2004) EMBO Rep , vol.5 , pp. 351-355
    • Filhol, O.1    Martiel, J.L.2    Cochet, C.3
  • 10
    • 0031600914 scopus 로고    scopus 로고
    • On the physiological role of casein kinase II in Saccharomyces cerevisiae
    • Glover CVC (1998) On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog Nucleic Acid Res Mol Biol 59: 95-133.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.59 , pp. 95-133
    • Glover, C.V.C.1
  • 11
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9: 576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 12
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members
    • Hanks SK, Quinn AM (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200: 38-62.
    • (1991) Methods Enzymol , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 13
    • 58249139330 scopus 로고
    • Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae
    • Hanna DE, Rethinaswamy A, Glover CVC (1995) Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J Biochem 10: 5869-5877.
    • (1995) J Biochem , vol.10 , pp. 5869-5877
    • Hanna, D.E.1    Rethinaswamy, A.2    Glover, C.V.C.3
  • 14
    • 0027430998 scopus 로고
    • Casein kinases: pleiotropic mediators of cellular regulation
    • Issinger O-G (1993) Casein kinases: pleiotropic mediators of cellular regulation. Pharmacol Ther 59: 1-30.
    • (1993) Pharmacol Ther , vol.59 , pp. 1-30
    • Issinger, O-G.1
  • 15
    • 3343024236 scopus 로고    scopus 로고
    • Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2α
    • Kannan N, Neuwald AF (2004) Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2α. Protein Sci 13: 2059-2077.
    • (2004) Protein Sci , vol.13 , pp. 2059-2077
    • Kannan, N.1    Neuwald, A.F.2
  • 16
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models
    • Kopp J, Schwede T (2004) The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res 32: D230-D234.
    • (2004) Nucleic Acids Res , vol.32
    • Kopp, J.1    Schwede, T.2
  • 17
    • 0027997895 scopus 로고
    • The growth of research on protein phosphorylation
    • Krebs EG (1994) The growth of research on protein phosphorylation. Trends Biochem Sci 19: 439-444.
    • (1994) Trends Biochem Sci , vol.19 , pp. 439-444
    • Krebs, E.G.1
  • 18
    • 33744949378 scopus 로고    scopus 로고
    • Yeast transcription elongation factor - Elf1 is phosphorylated and interact with protein kinase CK2
    • Kubiński K, Zieliński R, Hellman U, Mazur E, Szyszka R (2006) Yeast transcription elongation factor - Elf1 is phosphorylated and interact with protein kinase CK2. J Biochem Mol Biol 39: 311-318.
    • (2006) J Biochem Mol Biol , vol.39 , pp. 311-318
    • Kubiński, K.1    Zieliński, R.2    Hellman, U.3    Mazur, E.4    Szyszka, R.5
  • 19
    • 33846468333 scopus 로고    scopus 로고
    • Yeast holoenzyme of protein kinase CK2 requires both β and β′ regulatory subunits for its activity
    • Kubiński K, Domańska K, Sajnaga E, Mazur E, Zieliński R, Szyszka R (2007) Yeast holoenzyme of protein kinase CK2 requires both β and β′ regulatory subunits for its activity. Mol Cell Biochem 295: 229-235.
    • (2007) Mol Cell Biochem , vol.295 , pp. 229-235
    • Kubiński, K.1    Domańska, K.2    Sajnaga, E.3    Mazur, E.4    Zieliński, R.5    Szyszka, R.6
  • 20
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
    • Litchfield DW (2003) Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 369: 1-15.
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 21
    • 0027722138 scopus 로고
    • Casein kinase II in signal transduction and cell cycle regulation
    • Litchfield DW, Lüscher B (1993) Casein kinase II in signal transduction and cell cycle regulation. Mol Cell Biochem 127/128: 187-200.
    • (1993) Mol Cell Biochem , vol.127-128 , pp. 187-200
    • Litchfield, D.W.1    Lüscher, B.2
  • 23
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2
    • Meggio F, Pinna LA (2003) One-thousand-and-one substrates of protein kinase CK2. FASEB J 17: 349-368.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 24
    • 0023050184 scopus 로고
    • Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme
    • Meggio F, Grankowski N, Kudlicki W, Szyszka R, Ga{ogonek}sior E, Pinna LA (1986) Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme. Eur J Biochem 159: 31-38.
    • (1986) Eur J Biochem , vol.159 , pp. 31-38
    • Meggio, F.1    Grankowski, N.2    Kudlicki, W.3    Szyszka, R.4    Gasior, E.5    Pinna, L.A.6
  • 25
    • 0025060131 scopus 로고
    • Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase-2 and casein kinase-1
    • Meggio F, Shugar D, Pinna LA (1990) Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase-2 and casein kinase-1. Eur J Biochem 187: 89-94.
    • (1990) Eur J Biochem , vol.187 , pp. 89-94
    • Meggio, F.1    Shugar, D.2    Pinna, L.A.3
  • 27
    • 0035476623 scopus 로고    scopus 로고
    • Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme
    • Niefind K, Guerra B, Ermakowa I, Issinger O-G (2001) Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20: 5320-5331.
    • (2001) EMBO J , vol.20 , pp. 5320-5331
    • Niefind, K.1    Guerra, B.2    Ermakowa, I.3    Issinger, O-G.4
  • 28
    • 16844370286 scopus 로고    scopus 로고
    • Order or chaos? An evaluation of the regulation of protein kinase CK2
    • Olsten MEK, Litchfield DW (2004) Order or chaos? An evaluation of the regulation of protein kinase CK2. Biochem Cell Biol 82: 681-693.
    • (2004) Biochem Cell Biol , vol.82 , pp. 681-693
    • Olsten, M.E.K.1    Litchfield, D.W.2
  • 29
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: a challenge to canons
    • Pinna LA (2002) Protein kinase CK2: a challenge to canons. J Cell Sci 115: 3873-3878.
    • (2002) J Cell Sci , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 30
    • 0032489364 scopus 로고    scopus 로고
    • Temperature sensitive mutations of the CKA1 gene reveal a role for casein kinase CKII in maintenace of cell polarity in Saccharomyces cerevisiae
    • Rethinaswamy A, Birnbaum MJ, Glover CVC (1998) Temperature sensitive mutations of the CKA1 gene reveal a role for casein kinase CKII in maintenace of cell polarity in Saccharomyces cerevisiae. J Biol Chem 273: 5869-6877.
    • (1998) J Biol Chem , vol.273 , pp. 5869-6877
    • Rethinaswamy, A.1    Birnbaum, M.J.2    Glover, C.V.C.3
  • 31
    • 0037855971 scopus 로고    scopus 로고
    • Purification and characterization of recombinant protein kinase CK2 from Zea mays expressed in Escherichia coli
    • Riera M, Pages M, Issinger O-G, Guerra B (2003) Purification and characterization of recombinant protein kinase CK2 from Zea mays expressed in Escherichia coli. Protein Exp Purif 29: 24-32.
    • (2003) Protein Exp Purif , vol.29 , pp. 24-32
    • Riera, M.1    Pages, M.2    Issinger, O.-G.3    Guerra, B.4
  • 32
    • 0030817009 scopus 로고    scopus 로고
    • Mutational analysis of residues implicated in the interaction between protein kinase CK2 and peptide substrates
    • Sarno S, Vaglio P, Marin O, Issinger O-G, Ruffato K, Pinna LA (1997) Mutational analysis of residues implicated in the interaction between protein kinase CK2 and peptide substrates. Biochemistry 36: 11717-11724.
    • (1997) Biochemistry , vol.36 , pp. 11717-11724
    • Sarno, S.1    Vaglio, P.2    Marin, O.3    Issinger, O-G.4    Ruffato, K.5    Pinna, L.A.6
  • 34
    • 0037151103 scopus 로고    scopus 로고
    • Unique activation mechanism of protein kinase CK2
    • Sarno S, Ghisellini P, Pinna LA (2002b) Unique activation mechanism of protein kinase CK2. J Biol Chem 277: 22509-22514.
    • (2002) J Biol Chem , vol.277 , pp. 22509-22514
    • Sarno, S.1    Ghisellini, P.2    Pinna, L.A.3
  • 38
    • 1642362308 scopus 로고    scopus 로고
    • Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast
    • Schaerer-Brodbeck C, Riezman H (2003) Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast. FEMS Yeast Res 4: 37-49.
    • (2003) FEMS Yeast Res , vol.4 , pp. 37-49
    • Schaerer-Brodbeck, C.1    Riezman, H.2
  • 41
    • 0345465657 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae
    • Tchórzewski M, Boguszewska A, Abramczyk D, Grankowski N (1999) Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae. Protein Expr Purif 15: 40-47.
    • (1999) Protein Expr Purif , vol.15 , pp. 40-47
    • Tchórzewski, M.1    Boguszewska, A.2    Abramczyk, D.3    Grankowski, N.4
  • 42
    • 0026039891 scopus 로고
    • Casein kinase I and II - multipotential serine protein kinases: structure, function, and regulation
    • Tuazon PT, Traugh J (1991) Casein kinase I and II - multipotential serine protein kinases: structure, function, and regulation. Adv Second Messenger Phosphoprotein Res 23: 123-164.
    • (1991) Adv Second Messenger Phosphoprotein Res , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.2
  • 43
    • 0030062446 scopus 로고    scopus 로고
    • Mapping the residues of protein kinase CK2α subunit responsible for responsiveness to polyanionic inhibitors
    • Vaglio P, Sarno S, Marin O, Meggio F, Issinger O-G, Pinna LA (1996) Mapping the residues of protein kinase CK2α subunit responsible for responsiveness to polyanionic inhibitors. FEBS Lett 380: 25-28.
    • (1996) FEBS Lett , vol.380 , pp. 25-28
    • Vaglio, P.1    Sarno, S.2    Marin, O.3    Meggio, F.4    Issinger, O.-G.5    Pinna, L.A.6
  • 44
    • 0035670183 scopus 로고    scopus 로고
    • Response of cancer cells to molecular interruption of the CK2 signal
    • Wang H, Davis A, Yu S, Ahmed K (2001) Response of cancer cells to molecular interruption of the CK2 signal. Mol Cell Biochem 227: 167-174.
    • (2001) Mol Cell Biochem , vol.227 , pp. 167-174
    • Wang, H.1    Davis, A.2    Yu, S.3    Ahmed, K.4
  • 45
    • 0037716542 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive inhibitor of protein kinase CK2 from various sources
    • Zień P, Bretner M, Szyszka R, Shugar D (2003a) Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive inhibitor of protein kinase CK2 from various sources. Biochem Biophys Res Commun 306: 129-133.
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 129-133
    • Zień, P.1    Bretner, M.2    Szyszka, R.3    Shugar, D.4
  • 46
    • 0344552877 scopus 로고    scopus 로고
    • TBBz but not TBBt discriminates between two molecular forms of CK2 in vivo and its implications
    • Zień P, Abramczyk O, Domańska K, Bretner M, Szyszka R (2003b) TBBz but not TBBt discriminates between two molecular forms of CK2 in vivo and its implications. Biochem Biophys Res Commun 312: 623-628.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 623-628
    • Zień, P.1    Abramczyk, O.2    Domańska, K.3    Bretner, M.4    Szyszka, R.5


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