메뉴 건너뛰기




Volumn 312, Issue 3, 2003, Pages 623-628

TBBz but not TBBt discriminates between two molecular forms of CK2 in vivo and its implications

Author keywords

CK2 ; Halogenated benzimidazoles and benzotriazoles; In vivo phosphorylation; P1 P2 Proteins; Translation; Yeast

Indexed keywords

4,5,6,7 TETRABROMOBENZIMIDAZOLE; 4,5,6,7 TETRABROMOBENZOTRIAZOLE; 4,5,6,7-TETRABROMOBENZIMIDAZOLE; 4,5,6,7-TETRABROMOBENZOTRIAZOLE; BENZIMIDAZOLE DERIVATIVE; CASEIN KINASE II; GLYCINE CLEAVAGE SYSTEM; HOLOENZYME; P JL5 PROTEIN; P-JL5 PROTEIN; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; PROTEIN SERINE THREONINE KINASE; PYRROLE DERIVATIVE; RAP PROTEIN; RIBOSOME PROTEIN; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0344552877     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.10.165     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0029685972 scopus 로고    scopus 로고
    • The NTP phosphate donor in kinase reactions: Is ATP a monopolist?
    • Shugar D. The NTP phosphate donor in kinase reactions: is ATP a monopolist? Acta Biochim. Pol. 43:1996;9-24.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 9-24
    • Shugar, D.1
  • 2
    • 0031600914 scopus 로고    scopus 로고
    • On the physiological role of casein kinase II in Saccharomyces cerevisiae
    • Glover C.V.C. On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog. Nucleic Acid Res. Mol. Biol. 59:1998;95-133.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.59 , pp. 95-133
    • Glover, C.V.C.1
  • 3
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F., Pinna L.A. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17:2003;349-368.
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 4
    • 0036493241 scopus 로고    scopus 로고
    • Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo
    • Majumdar R., Bandyopadhyay A., Deng H., Maitra U. Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo. Nucleic Acids Res. 30:2002;1154-1162.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1154-1162
    • Majumdar, R.1    Bandyopadhyay, A.2    Deng, H.3    Maitra, U.4
  • 5
    • 0033056148 scopus 로고    scopus 로고
    • A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII
    • Sheu G.T., Traugh J.A. A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII. Mol. Cell. Biochem. 191:1999;181-186.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 181-186
    • Sheu, G.T.1    Traugh, J.A.2
  • 6
    • 0032508493 scopus 로고    scopus 로고
    • Phosphorylation of the translational regulator, PHAS-I, by protein kinase CK2
    • Fadden P., Haystead T.A.J., Lawrence J.C. Jr. Phosphorylation of the translational regulator, PHAS-I, by protein kinase CK2. FEBS Lett. 435:1998;105-109.
    • (1998) FEBS Lett. , vol.435 , pp. 105-109
    • Fadden, P.1    Haystead, T.A.J.2    Lawrence Jr., J.C.3
  • 7
    • 0025826696 scopus 로고
    • Ribosomal proteins P0, P1, and P2 are phosphorylated by casein kinase II at their conserved carboxyl termini
    • Hasler P., Brot N., Weissbach H., Parnassa A.P., Elkon K.B. Ribosomal proteins P0, P1, and P2 are phosphorylated by casein kinase II at their conserved carboxyl termini. J. Biol. Chem. 266:1991;13815-13820.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13815-13820
    • Hasler, P.1    Brot, N.2    Weissbach, H.3    Parnassa, A.P.4    Elkon, K.B.5
  • 8
    • 0021765023 scopus 로고
    • Detection of type-2 casein kinase and its endogenous substrates in the components of the microsomal fraction of rat liver
    • Meggio F., Brunati A.M., Donella-Deana A., Pinna L.A. Detection of type-2 casein kinase and its endogenous substrates in the components of the microsomal fraction of rat liver. Eur. J. Biochem. 138:1984;379-385.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 379-385
    • Meggio, F.1    Brunati, A.M.2    Donella-Deana, A.3    Pinna, L.A.4
  • 9
    • 0017021218 scopus 로고
    • Ribosomal protein as substrate for a GTP-dependent protein kinase from yeast
    • Kudlicki W., Grankowski N., Gasior E. Ribosomal protein as substrate for a GTP-dependent protein kinase from yeast. Mol. Biol. Rep. 3:1976;121-129.
    • (1976) Mol. Biol. Rep. , vol.3 , pp. 121-129
    • Kudlicki, W.1    Grankowski, N.2    Gasior, E.3
  • 10
    • 0017644960 scopus 로고
    • Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase
    • Issinger O.-G. Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase. Biochim. Biophys. Acta. 477:1977;185-189.
    • (1977) Biochim. Biophys. Acta , vol.477 , pp. 185-189
    • Issinger, O.-G.1
  • 11
    • 0029686290 scopus 로고    scopus 로고
    • The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery
    • Ballesta J.P.G., Remacha M. The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery. Prog. Nucleic Acid Res. Mol. Biol. 55:1996;157-193.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.55 , pp. 157-193
    • Ballesta, J.P.G.1    Remacha, M.2
  • 12
    • 0025988131 scopus 로고
    • The primary structure of rat ribosomal proteins P0, P1 and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins
    • Wool I.G., Chan Y.-L., Gluck A., Suzuki K. The primary structure of rat ribosomal proteins P0, P1 and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie. 73:1991;861-870.
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.G.1    Chan, Y.-L.2    Gluck, A.3    Suzuki, K.4
  • 13
    • 0032579887 scopus 로고    scopus 로고
    • The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae
    • Planta R.J., Mager W.H. The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast. 14:1999;471-477.
    • (1999) Yeast , vol.14 , pp. 471-477
    • Planta, R.J.1    Mager, W.H.2
  • 14
    • 0030711636 scopus 로고    scopus 로고
    • Phosphorylation of the acidic ribosomal P proteins in Saccharomyces cerevisiae: A reappraisal
    • Zambrano R., Briones E., Remacha M., Ballesta J.P.G. Phosphorylation of the acidic ribosomal P proteins in Saccharomyces cerevisiae: a reappraisal. Biochemistry. 36:1997;14436-14439.
    • (1997) Biochemistry , vol.36 , pp. 14436-14439
    • Zambrano, R.1    Briones, E.2    Remacha, M.3    Ballesta, J.P.G.4
  • 15
    • 0031299580 scopus 로고    scopus 로고
    • The phosphorylation sites of ribosomal P proteins from Saccharomyces cerevisiae cells by endogenous CK-2, PK60S and RAP protein kinases
    • Boguszewska A., Szyszka R., Grankowski N. The phosphorylation sites of ribosomal P proteins from Saccharomyces cerevisiae cells by endogenous CK-2, PK60S and RAP protein kinases. Acta Biochim. Pol. 44:1997;191-200.
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 191-200
    • Boguszewska, A.1    Szyszka, R.2    Grankowski, N.3
  • 16
    • 0032564302 scopus 로고    scopus 로고
    • Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation
    • Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G. Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation. Biochemistry. 37:1998;16606-16620.
    • (1998) Biochemistry , vol.37 , pp. 16606-16620
    • Rodriguez-Gabriel, M.A.1    Remacha, M.2    Ballesta, J.P.G.3
  • 17
    • 0029925323 scopus 로고
    • RAP kinase, a new enzyme phosphorylating the acidic P proteins from Saccharomyces cerevisiae
    • Szyszka R., Bou G., Ballesta J.P.G. RAP kinase, a new enzyme phosphorylating the acidic P proteins from Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1293:1995;213-221.
    • (1995) Biochim. Biophys. Acta , vol.1293 , pp. 213-221
    • Szyszka, R.1    Bou, G.2    Ballesta, J.P.G.3
  • 18
    • 0034163306 scopus 로고    scopus 로고
    • Ribosomal stalk protein phosphorylating activities in Saccharomyces cerevisiae
    • Bou G., Remacha M., Ballesta J.P.G. Ribosomal stalk protein phosphorylating activities in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 375:2001;83-89.
    • (2001) Arch. Biochem. Biophys. , vol.375 , pp. 83-89
    • Bou, G.1    Remacha, M.2    Ballesta, J.P.G.3
  • 20
    • 0037716542 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive potent inhibitor of protein kinase CK2 from various sources
    • Zień P., Bretner M., Zasta̧piło K., Szyszka R., Shugar D. Selectivity of 4,5,6,7-tetrabromobenzimidazole as an ATP-competitive potent inhibitor of protein kinase CK2 from various sources. Biochem. Biophys. Res. Commun. 306:2003;129-133.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 129-133
    • Zień, P.1    Bretner, M.2    Zasta̧piło, K.3    Szyszka, R.4    Shugar, D.5
  • 21
    • 0014183819 scopus 로고
    • Ribosomal precursor RNA in Saccharomyces carlsbergensis
    • Retel J., Planta R.J. Ribosomal precursor RNA in Saccharomyces carlsbergensis. Eur. J. Biochem. 3:1967;248-258.
    • (1967) Eur. J. Biochem. , vol.3 , pp. 248-258
    • Retel, J.1    Planta, R.J.2
  • 22
    • 0021728955 scopus 로고
    • Phosphorylation of ribosomal proteins during differentiation of Saccharomyces cerevisiae
    • Szyszka R., G a sior E. Phosphorylation of ribosomal proteins during differentiation of Saccharomyces cerevisiae. Acta Biochim. Pol. 31:1984;375-382.
    • (1984) Acta Biochim. Pol. , vol.31 , pp. 375-382
    • Szyszka, R.1    Sior E, G.A.2
  • 23
    • 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., Gsior E., Pinna L.A. Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme. Eur. J. Biochem. 159:1986;31-38.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 31-38
    • Meggio, F.1    Grankowski, N.2    Kudlicki, W.3    Szyszka, R.4    Gsior, E.5    Pinna, L.A.6
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72:1970;248-254.
    • (1970) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0033574223 scopus 로고    scopus 로고
    • Structural features underlying the unusual mode of calmodulin phosphorylation by protein kinase CK2: A study with synthetic calmodulin fragments
    • Marin O., Meggio F., Pinna L.A. Structural features underlying the unusual mode of calmodulin phosphorylation by protein kinase CK2: a study with synthetic calmodulin fragments. Biochem. Biophys. Res. Commun. 256:1999;442-446.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 442-446
    • Marin, O.1    Meggio, F.2    Pinna, L.A.3
  • 27
    • 0026453351 scopus 로고
    • Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle
    • Kikkawa U., Mann S.K., Firtel R.A., Hunter T. Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle. Mol. Cell. Biol. 12:1992;5711-5723.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5711-5723
    • Kikkawa, U.1    Mann, S.K.2    Firtel, R.A.3    Hunter, T.4
  • 28
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • Pinna L.A. Protein kinase CK2: a challenge to canons. J. Cell Sci. 115:2002;3873-3878.
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 29
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield D.W. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 369:2003;1-15.
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 30
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • Ahmed K., Gerber D.A., Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. TIBS. 12:2002;226-230.
    • (2002) TIBS , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 31
    • 0019428163 scopus 로고
    • Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosomes
    • Sanchez-Madrid F., Vidales F.J., Ballesta J.P.G. Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosomes. Eur. J. Biochem. 114:1981;609-613.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 609-613
    • Sanchez-Madrid, F.1    Vidales, F.J.2    Ballesta, J.P.G.3
  • 32
    • 0017256641 scopus 로고
    • The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins
    • Zinker S., Warner J.R.J. The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins. J. Biol. Chem. 251:1976;1799-1807.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1799-1807
    • Zinker, S.1    Warner, J.R.J.2
  • 33
    • 0002623943 scopus 로고
    • Control of ribosome biosynthesis in plant cell cultures under shock conditions
    • Sharf K.-D., Nover L. Control of ribosome biosynthesis in plant cell cultures under shock conditions. Biochem. Biophys. Acta. 909:1987;44-57.
    • (1987) Biochem. Biophys. Acta , vol.909 , pp. 44-57
    • Sharf, K.-D.1    Nover, L.2
  • 34
    • 0022369647 scopus 로고
    • Evidence for exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver
    • Tsurugi K., Ogata K.J. Evidence for exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J. Biochem. 98:1985;405-416.
    • (1985) J. Biochem. , vol.98 , pp. 405-416
    • Tsurugi, K.1    Ogata, K.J.2
  • 35
    • 0035999791 scopus 로고    scopus 로고
    • Structure and function of the acidic ribosomal stalk proteins
    • Wahl M.C., Möller W. Structure and function of the acidic ribosomal stalk proteins. Curr. Protein Pept. Sci. 3:2002;93-106.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 93-106
    • Wahl, M.C.1    Möller, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.