메뉴 건너뛰기




Volumn 296, Issue 5, 2002, Pages 1366-1371

Acidophilic character of yeast PID261/BUD32, a putative ancestor of eukaryotic protein kinases

Author keywords

Archaea; Bud32; Casein kinase; CK2 subunit; Evolution; PiD261; Protein kinase; Protein phosphorylation; Yeast; YGR262c

Indexed keywords

ACID PROTEIN; PEPTIDE DERIVATIVE; PROLINE; PROTEIN BUD32; PROTEIN KINASE; PROTEIN PID261; UNCLASSIFIED DRUG;

EID: 0036387181     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02090-9     Document Type: Article
Times cited : (14)

References (28)
  • 1
    • 0031026008 scopus 로고    scopus 로고
    • The protein kinases of budding yeast: Six score and more
    • T. Hunter, G.D. Plowman, The protein kinases of budding yeast: six score and more, Trends Biochem. Sci. 22 (1997) 18-22.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 18-22
    • Hunter, T.1    Plowman, G.D.2
  • 2
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinases of Caenorhabditis elegans: A model for signal transduction in multicellular organisms
    • G.D. Plowman, S. Sudarsanam, J. Bingham, D. Whyte, T. Hunter, The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms, Proc. Natl. Acad. Sci. USA 96 (1999) 13603-13610.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13603-13610
    • Plowman, G.D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 3
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • J.C. Venter, M.D. Adams, E.W. Myers, E.W. Li, et al., The sequence of the human genome, Science 291 (2001) 1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1    Adams, M.D.2    Myers, E.W.3    Li, E.W.4
  • 4
    • 0029743605 scopus 로고    scopus 로고
    • Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation
    • P.J. Kennelly, M. Potts, Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation, J. Bacteriol. 178 (1996) 4759-4764.
    • (1996) J. Bacteriol. , vol.178 , pp. 4759-4764
    • Kennelly, P.J.1    Potts, M.2
  • 5
    • 0028964131 scopus 로고
    • Identification of a eukaryotic-like protein kinase gene in Archaebacteria
    • R.F. Smith, K.Y. King, Identification of a eukaryotic-like protein kinase gene in Archaebacteria, Protein Sci. 4 (1995) 126-129.
    • (1995) Protein Sci. , vol.4 , pp. 126-129
    • Smith, R.F.1    King, K.Y.2
  • 6
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • L.A. Pinna, M. Ruzzene, How do protein kinases recognize their substrates?, Biochim. Biophys. Acta 1314 (1996) 191-225.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 7
    • 0030874691 scopus 로고    scopus 로고
    • Biochemical evidence that Saccharomyces cerevisiae YGR262c gene required for normal growth, encodes a novel Ser/Thr-specific protein kinase
    • S. Stocchetto, O. Marin, G. Carignani, L.A. Pinna, Biochemical evidence that Saccharomyces cerevisiae YGR262c gene required for normal growth, encodes a novel Ser/Thr-specific protein kinase, FEBS Lett. 414 (1997) 171-175.
    • (1997) FEBS Lett. , vol.414 , pp. 171-175
    • Stocchetto, S.1    Marin, O.2    Carignani, G.3    Pinna, L.A.4
  • 8
    • 0035162931 scopus 로고    scopus 로고
    • A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae
    • L. Ni, M. Snyder, A Genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae, Mol. Biol. Cell 12 (2001) 2147-2170.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2147-2170
    • Ni, L.1    Snyder, M.2
  • 9
    • 0033954495 scopus 로고    scopus 로고
    • Inactivation of six genes from chromosomes VII of Saccharomyces cerevisiae and basic phenotypic analysis of the mutant strains
    • G. Sartori, G. Mazzotta, S. Stocchetto, A. Pavanello, G. Carignani, Inactivation of six genes from chromosomes VII of Saccharomyces cerevisiae and basic phenotypic analysis of the mutant strains, Yeast 16 (2000) 255-265.
    • (2000) Yeast , vol.16 , pp. 255-265
    • Sartori, G.1    Mazzotta, G.2    Stocchetto, S.3    Pavanello, A.4    Carignani, G.5
  • 10
    • 0037196946 scopus 로고    scopus 로고
    • Systematic analysis of sporulation phenotypes in 624 non-lethal homozygous deletion strains of Saccharomyces cerevisiae
    • P. Briza, E. Bogengruber, A. Thur, M. Rutzler, M. Munsterkotter, I.W. Dawes, M. Breitenbach, Systematic analysis of sporulation phenotypes in 624 non-lethal homozygous deletion strains of Saccharomyces cerevisiae, Yeast 19 (2002) 403-422.
    • (2002) Yeast , vol.19 , pp. 403-422
    • Briza, P.1    Bogengruber, E.2    Thur, A.3    Rutzler, M.4    Munsterkotter, M.5    Dawes, I.W.6    Breitenbach, M.7
  • 11
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the "eukaryotic" protein kinase superfamily
    • C.J. Leonard, L. Aravind, E.V. Koonin, Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily, Genome Res. 10 (1998) 1038-1047.
    • (1998) Genome Res. , vol.10 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 12
    • 0035941268 scopus 로고    scopus 로고
    • Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes
    • Y. Abe, S. Matsumoto, S. Wei, K. Nezu, A. Miyoshi, K. Kito, N. Ueda, K. Shigemoto, Y. Hitsumoto, J. Nikawa, Y. Enomoto, Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes, J. Biol. Chem. 276 (2001) 44003-44011.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44003-44011
    • Abe, Y.1    Matsumoto, S.2    Wei, S.3    Nezu, K.4    Miyoshi, A.5    Kito, K.6    Ueda, N.7    Shigemoto, K.8    Hitsumoto, Y.9    Nikawa, J.10    Enomoto, Y.11
  • 14
    • 0033548655 scopus 로고    scopus 로고
    • Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fcr Protein-tyrosine kinase
    • A.M. Brunati, A. Donella-Deana, P. James, M. Quadroni, A. Contri, O. Marin, L.A. Pinna, Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fcr Protein-tyrosine kinase, J. Biol. Chem. 274 (1999) 7557-7564.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7557-7564
    • Brunati, A.M.1    Donella-Deana, A.2    James, P.3    Quadroni, M.4    Contri, A.5    Marin, O.6    Pinna, L.A.7
  • 15
    • 0026474670 scopus 로고
    • Casein kinase-2 structure-function relationship: Creation of a set of mutants of the b subunit that variably surrogate the wildtype β subunit function
    • B. Boldyreff, F. Meggio, L.A. Pinna, O.G. Issinger, Casein kinase-2 structure-function relationship: creation of a set of mutants of the β subunit that variably surrogate the wildtype b subunit function, Biochem. Biophys. Res. Commun. 188 (1992) 228-234.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 228-234
    • Boldyreff, B.1    Meggio, F.2    Pinna, L.A.3    Issinger, O.G.4
  • 16
    • 0028036142 scopus 로고
    • Recombinant human casein kinase II. A study with the complete set of subunits (α′ and β), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme
    • L. Bodenbach, J. Fauss, A. Robitzki, A. Krehan, P. Lorenz, F.J. Lozeman, W. Pyerin, Recombinant human casein kinase II. A study with the complete set of subunits (α′ and β), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme, Eur. J. Biochem. 220 (1994) 263-273.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 263-273
    • Bodenbach, L.1    Fauss, J.2    Robitzki, A.3    Krehan, A.4    Lorenz, P.5    Lozeman, F.J.6    Pyerin, W.7
  • 17
    • 0034646835 scopus 로고    scopus 로고
    • GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase
    • A.M. Brunati, A. Contri, M. Muenchbach, P. James, O. Marin, L.A. Pinna, GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase, FEBS Lett. 14 (2000) 151-155.
    • (2000) FEBS Lett. , vol.14 , pp. 151-155
    • Brunati, A.M.1    Contri, A.2    Muenchbach, M.3    James, P.4    Marin, O.5    Pinna, L.A.6
  • 18
    • 0030046449 scopus 로고    scopus 로고
    • Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites
    • A. Donella-Deana, P. James, W. Staudenmann, L. Cesaro, O. Marin, A.M. Brunati, M. Ruzzene, L.A. Pinna, Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites, Eur. J. Biochem. 235 (1996) 18-25.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 18-25
    • Donella-Deana, A.1    James, P.2    Staudenmann, W.3    Cesaro, L.4    Marin, O.5    Brunati, A.M.6    Ruzzene, M.7    Pinna, L.A.8
  • 19
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • G.B. Fields, R.L. Noble, Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids, Int. J. Pept. Protein Res. 35(1990) 161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 20
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • D.S. King, C.G. Fields, G.B. Fields, A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis, Int. J. Pept. Protein Res. 36 (1990) 255-266.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 21
    • 0030921077 scopus 로고    scopus 로고
    • Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 β-subunit
    • O. Marin, F. Meggio, S. Sarno, L.A. Pinna, Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 β-subunit, Biochemistry 36 (1997) 7192-7198.
    • (1997) Biochemistry , vol.36 , pp. 7192-7198
    • Marin, O.1    Meggio, F.2    Sarno, S.3    Pinna, L.A.4
  • 22
    • 17544377840 scopus 로고    scopus 로고
    • Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis
    • S. Sarno, P. Vaglio, F. Meggio, O.G. Issinger, L.A. Pinna, Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis, J. Biol. Chem. 271 (1996) 10595-10601.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10595-10601
    • Sarno, S.1    Vaglio, P.2    Meggio, F.3    Issinger, O.G.4    Pinna, L.A.5
  • 23
    • 0027237630 scopus 로고
    • The autophosphorylation and p34cdc2 phosphorylation sites of casein kinase-2 β-subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme
    • F. Meggio, B. Boldyreff, O.G. Issinger, L.A. Pinna, The autophosphorylation and p34cdc2 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.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 223-225
    • Meggio, F.1    Boldyreff, B.2    Issinger, O.G.3    Pinna, L.A.4
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schagger, G. von Jagow, Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166 (1987) 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 26
    • 0037161965 scopus 로고    scopus 로고
    • Phosphorylation regulates the stability of the regulatory CK2b subunit
    • C. Zhang, G. Vilk, D.A. Canton, D.W. Litchfield, Phosphorylation regulates the stability of the regulatory CK2b subunit, Oncogene 21 (2002) 3754-3764.
    • (2002) Oncogene , vol.21 , pp. 3754-3764
    • Zhang, C.1    Vilk, G.2    Canton, D.A.3    Litchfield, D.W.4
  • 27
    • 0026508869 scopus 로고
    • Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme
    • F. Meggio, B. Boldyreff, O. Marin, L.A. Pinna, O.G. Issinger, Role of the b subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme, Eur. J. Biochem. 204 (1992) 293-297.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 293-297
    • Meggio, F.1    Boldyreff, B.2    Marin, O.3    Pinna, L.A.4    Issinger, O.G.5
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, T.J. Gibson, CLUSTAL W. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.