메뉴 건너뛰기




Volumn 6, Issue 5, 2004, Pages 453-462

Isolation and characterization of ornithine decarboxylase gene from flounder (Paralichthys olivaceus)

Author keywords

Flounder (Paralichthys olivaceus); Ornithine decarboxylase (ODC); Pyridoxal 5 phosphate (PLP)

Indexed keywords

BIOLOGICAL ORGANS; CHROMATOGRAPHIC ANALYSIS; CLONING; ECOSYSTEMS; ENZYMES; GENETIC ENGINEERING; OCEAN HABITATS;

EID: 16844384618     PISSN: 14362228     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10126-004-4100-3     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 0034614359 scopus 로고    scopus 로고
    • Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: Structual insights to antizyme binding
    • J.J. Almrud M.A. Oliveira A.D. Kern N.V. Grishin M.A. Philips M.L. Hackert 2000 Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: structual insights to antizyme binding J Mol Biol 295 7 16
    • (2000) J Mol Biol , vol.295 , pp. 7-16
    • Almrud, J.J.1    Oliveira, M.A.2    Kern, A.D.3    Grishin, N.V.4    Philips, M.A.5    Hackert, M.L.6
  • 2
    • 0025241359 scopus 로고
    • Post-transcriptional regulation of ornithine decarboxylase in Xenopus laevis oocytes
    • T. Bassez J. Paris R Omilli C. Dorel H.B. Osborne 1990 Post-transcriptional regulation of ornithine decarboxylase in Xenopus laevis oocytes Development 110 955 962
    • (1990) Development , vol.110 , pp. 955-962
    • Bassez, T.1    Paris, J.2    Omilli, R.3    Dorel, C.4    Osborne, H.B.5
  • 3
    • 0035056853 scopus 로고    scopus 로고
    • Tissue-specific expression of an ornithine decarboxylase paralogue, XODC2, in Xenopus laevis
    • Y. Cao H. Zhao T. Hollemann Y. Chen H. Grunz 2001 Tissue-specific expression of an ornithine decarboxylase paralogue, XODC2, in Xenopus laevis Mech Dev 102 243 246
    • (2001) Mech Dev , vol.102 , pp. 243-246
    • Cao, Y.1    Zhao, H.2    Hollemann, T.3    Chen, Y.4    Grunz, H.5
  • 4
    • 0026758194 scopus 로고
    • Mechanism of regulation of ornithine decarboxylase gene expression by asparagines in a variant mouse neuroblastoma cell line
    • Z.P. Chen K.Y. Chen 1992 Mechanism of regulation of ornithine decarboxylase gene expression by asparagines in a variant mouse neuroblastoma cell line J Biol Chem 267 6946 6951
    • (1992) J Biol Chem , vol.267 , pp. 6946-6951
    • Chen, Z.P.1    Chen, K.Y.2
  • 5
    • 0032767639 scopus 로고    scopus 로고
    • CDNA encoding nm23/NDP kinase gene from Korean tiger shark Scyliorhinus torazame
    • J.J. Cho J.H. Lee S-K. Kim T-J. Choi Y.T. Kim 1999 cDNA encoding nm23/NDP kinase gene from Korean tiger shark Scyliorhinus torazame Mar Biotechnol 1 131 136
    • (1999) Mar Biotechnol , vol.1 , pp. 131-136
    • Cho, J.J.1    Lee, J.H.2    Kim, S.-K.3    Choi, T.-J.4    Kim, Y.T.5
  • 6
    • 0035972177 scopus 로고    scopus 로고
    • CDNA for an immune response gene encoding low molecular weight polypeptide from flounder, Paralichthys olivaceus
    • J.J. Cho B.K. Sung J.H. Lee J-K. Chung T-J. Choi Y.T. Kim 2001 cDNA for an immune response gene encoding low molecular weight polypeptide from flounder, Paralichthys olivaceus Mol Cells 11 226 230
    • (2001) Mol Cells , vol.11 , pp. 226-230
    • Cho, J.J.1    Sung, B.K.2    Lee, J.H.3    Chung, J.-K.4    Choi, T.-J.5    Kim, Y.T.6
  • 8
    • 0035291218 scopus 로고    scopus 로고
    • Regulation of cellular polyamines by antizyme
    • P. Coffino 2001 Regulation of cellular polyamines by antizyme Nat Rev Mol Cell Biol 2 188 194
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 188-194
    • Coffino, P.1
  • 9
  • 10
    • 0027965970 scopus 로고
    • Rapid exchange of subunits of mammalian ornithine decarboxylase
    • C.S. Coleman B.A. Stanley R. Viswanath A.E. Pegg 1994 Rapid exchange of subunits of mammalian ornithine decarboxylase J Biol Chem 269 3155 3158
    • (1994) J Biol Chem , vol.269 , pp. 3155-3158
    • Coleman, C.S.1    Stanley, B.A.2    Viswanath, R.3    Pegg, A.E.4
  • 11
    • 0020579390 scopus 로고
    • Protein blotting: Principles and application
    • J.M. Gershoni G.E. Palade 1983 Protein blotting: principles and application Anal Biochem 131 1 15
    • (1983) Anal Biochem , vol.131 , pp. 1-15
    • Gershoni, J.M.1    Palade, G.E.2
  • 12
    • 0025277641 scopus 로고
    • The 5'- and 3'-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency
    • A. Grens I.E. Scheffler 1990 The 5'- and 3'-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency J Biol Chem 265 11810 11816
    • (1990) J Biol Chem , vol.265 , pp. 11810-11816
    • Grens, A.1    Scheffler, I.E.2
  • 13
    • 0024829782 scopus 로고
    • Nucleotide sequence of the Chinese hamster ornithine decarboxylase gene
    • A. Grens C. Steglich R. Pilz I.E. Scheffler 1989 Nucleotide sequence of the Chinese hamster ornithine decarboxylase gene Nucleic Acids Res 17 10497
    • (1989) Nucleic Acids Res , vol.17 , pp. 10497
    • Grens, A.1    Steglich, C.2    Pilz, R.3    Scheffler, I.E.4
  • 14
    • 0037064164 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase by antizymes and antizyme inhibitor in zebrafish (Danio rerio)
    • T. Hascilowicz N. Murai S. Matsufuji Y. Murakami 2002 Regulation of ornithine decarboxylase by antizymes and antizyme inhibitor in zebrafish (Danio rerio) Biochim Biophys Acta 1578 21 28
    • (2002) Biochim Biophys Acta , vol.1578 , pp. 21-28
    • Hascilowicz, T.1    Murai, N.2    Matsufuji, S.3    Murakami, Y.4
  • 15
    • 0028799607 scopus 로고
    • Rapid and regulated degradation of ornithine decarboxylase
    • S. Hayashi Y. Murakami 1995 Rapid and regulated degradation of ornithine decarboxylase Biochem J 306 1 10
    • (1995) Biochem J , vol.306 , pp. 1-10
    • Hayashi, S.1    Murakami, Y.2
  • 16
    • 0030052923 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme: A novel type of regulatory protein
    • S. Hayashi Y Murakmi S. Matsufuji 1996 Ornithine decarboxylase antizyme: a novel type of regulatory protein Trends Biochem Sci 21 27 30
    • (1996) Trends Biochem Sci , vol.21 , pp. 27-30
    • Hayashi, S.1    Murakmi, Y.2    Matsufuji, S.3
  • 17
    • 0025325255 scopus 로고
    • Molecular genetics of polyamin synthesis in eukaryotic cells
    • O. Heby L. Persson 1990 Molecular genetics of polyamin synthesis in eukaryotic cells Trends Biochem Sci 15 153 158
    • (1990) Trends Biochem Sci , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 18
    • 0024266259 scopus 로고
    • Feedback regulation of polyamine synthesis in Ehrlich ascites tumor cells: Analysis using nonmetabolizable derivatives of putrescine and spermine
    • I. Holm L. Persson O. Heby N. Seiler 1988 Feedback regulation of polyamine synthesis in Ehrlich ascites tumor cells: analysis using nonmetabolizable derivatives of putrescine and spermine Biochim Biophys Acta 972 239 248
    • (1988) Biochim Biophys Acta , vol.972 , pp. 239-248
    • Holm, I.1    Persson, L.2    Heby, O.3    Seiler, N.4
  • 19
    • 0026648982 scopus 로고
    • Alterations in mRNA translation as a mechanism for the modification of enzyme synthesis during evolution: The ornithine decarboxylase model
    • G. Johannes F.G. Berger 1992 Alterations in mRNA translation as a mechanism for the modification of enzyme synthesis during evolution: the ornithine decarboxylase model J Biol Chem 267 10108 10115
    • (1992) J Biol Chem , vol.267 , pp. 10108-10115
    • Johannes, G.1    Berger, F.G.2
  • 20
    • 0026618670 scopus 로고
    • Molecular cloning and sequence analysis of a chicken ornithine decarboxylase cDNA
    • R. Johnson G. Bulfield 1992 Molecular cloning and sequence analysis of a chicken ornithine decarboxylase cDNA Anim Genet 23 403 409
    • (1992) Anim Genet , vol.23 , pp. 403-409
    • Johnson, R.1    Bulfield, G.2
  • 21
    • 0021867425 scopus 로고
    • Nucleotide sequence of murine ornithine decarboxylase mRNA
    • C. Kahana D. Nathans 1985 Nucleotide sequence of murine ornithine decarboxylase mRNA Proc Natl Acad Sci U S A 82 1673 1677
    • (1985) Proc Natl Acad Sci U S a , vol.82 , pp. 1673-1677
    • Kahana, C.1    Nathans, D.2
  • 22
    • 0023372166 scopus 로고
    • Transcriptional activation of mammalian ornithine decarboxylase during stimulated growth
    • A. Katz C. Kahana 1987 Transcriptional activation of mammalian ornithine decarboxylase during stimulated growth Mol Cell Biol 7 2641 2643
    • (1987) Mol Cell Biol , vol.7 , pp. 2641-2643
    • Katz, A.1    Kahana, C.2
  • 23
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: Stereochemical implications of PLP-dependent amino acid decarboxylases
    • A.D. Kern M.A. Oliveira P. Coffino M.L. Hackert 1999 Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases Structure Fold Des 7 567 581
    • (1999) Structure Fold des , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.L.4
  • 24
    • 0345435939 scopus 로고    scopus 로고
    • Identification of an embryonic growth factor IGF-II from the central nervous system of the teleost, flounder, and its expressions in adult tissues
    • D.S. Kim Y.T Kim 1999 Identification of an embryonic growth factor IGF-II from the central nervous system of the teleost, flounder, and its expressions in adult tissues J Microbiol Biotechnol 9 113 118
    • (1999) J Microbiol Biotechnol , vol.9 , pp. 113-118
    • Kim, D.S.1    Kim, Y.T.2
  • 25
    • 0000600380 scopus 로고
    • Bacteriophage T7 gene 2.5 protein: An essential protein for DNA replication
    • Y.T. Kim C.C. Richardson 1993 Bacteriophage T7 gene 2.5 protein: an essential protein for DNA replication Proc Natl Acad Sci U S A 90 10173 10177
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 10173-10177
    • Kim, Y.T.1    Richardson, C.C.2
  • 26
    • 0028018381 scopus 로고
    • Acidic carboxyl-terminal domain of gene 2.5 protein of bacteriophage T7 is essential for protein-protein interactions
    • Y.T. Kim C.C. Richardson 1994 Acidic carboxyl-terminal domain of gene 2.5 protein of bacteriophage T7 is essential for protein-protein interactions J Biol Chem 269 5270 5278
    • (1994) J Biol Chem , vol.269 , pp. 5270-5278
    • Kim, Y.T.1    Richardson, C.C.2
  • 27
    • 0031031867 scopus 로고    scopus 로고
    • Recombinant brain 4-aminobutyrate aminotransferases: Overexpression, purification, and identification of Lys-330 at the active site
    • Y.T. Kim Y.H. Song J.E. Churchich 1997 Recombinant brain 4-aminobutyrate aminotransferases: overexpression, purification, and identification of Lys-330 at the active site Biochim Biophys Acta 1337 248 256
    • (1997) Biochim Biophys Acta , vol.1337 , pp. 248-256
    • Kim, Y.T.1    Song, Y.H.2    Churchich, J.E.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0035934299 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the interleukin-8 gene from flounder (Paralichthys olivaceus)
    • E-Y. Lee H-H. Park Y.T. Kim T-J. Choi 2001 Cloning and sequence analysis of the interleukin-8 gene from flounder (Paralichthys olivaceus) Gene 274 237 243
    • (2001) Gene , vol.274 , pp. 237-243
    • Lee, E.-Y.1    Park, H.-H.2    Kim, Y.T.3    Choi, T.-J.4
  • 30
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • X. Li P. Coffino 1993 Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein Mol Cell Biol 13 2377 2383
    • (1993) Mol Cell Biol , vol.13 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 33
    • 0022425793 scopus 로고
    • Role of antizyme in degradation of ornithine decarboxylase in HTC cells
    • Y. Murakami S. Hayashi 1985 Role of antizyme in degradation of ornithine decarboxylase in HTC cells Biochem J 226 893 896
    • (1985) Biochem J , vol.226 , pp. 893-896
    • Murakami, Y.1    Hayashi, S.2
  • 36
    • 0029042171 scopus 로고
    • Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis
    • A.L. Osterman L.N. Kinch N.V. Grishin M.A. Phillips 1995a Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis J Biol Chem 270 11797 11802
    • (1995) J Biol Chem , vol.270 , pp. 11797-11802
    • Osterman, A.L.1    Kinch, L.N.2    Grishin, N.V.3    Phillips, M.A.4
  • 38
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryotes
    • A.E. Pegg 1986 Recent advances in the biochemistry of polyamines in eukaryotes Biochem J 234 249 262
    • (1986) Biochem J , vol.234 , pp. 249-262
    • Pegg, A.E.1
  • 39
    • 0023862943 scopus 로고
    • Regulation of ornithine decarboxylase mRNA translation by polyamines: Studies using a cell-free system and a cell line with an amplified ornithine decarboxylase gene
    • L. Persson I. Holm O. Heby 1988 Regulation of ornithine decarboxylase mRNA translation by polyamines: studies using a cell-free system and a cell line with an amplified ornithine decarboxylase gene J Biol Chem 263 3528 3533
    • (1988) J Biol Chem , vol.263 , pp. 3528-3533
    • Persson, L.1    Holm, I.2    Heby, O.3
  • 40
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei: Implications for enzyme turnover and selective difluoromethylornithine inhibition
    • M.A. Phillips P. Coffino C.C. Wang 1987 Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei: implications for enzyme turnover and selective difluoromethylornithine inhibition J Biol Chem 262 8721 8727
    • (1987) J Biol Chem , vol.262 , pp. 8721-8727
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 41
    • 0026599430 scopus 로고
    • Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethyl ornithine: Characterization of sequence at the inhibitor and coenzyme binding sites
    • R. Poulin L. Lu B. Ackerman P. Bey A.E. Pegg 1992 Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethyl ornithine: characterization of sequence at the inhibitor and coenzyme binding sites J Biol Chem 267 150 158
    • (1992) J Biol Chem , vol.267 , pp. 150-158
    • Poulin, R.1    Lu, L.2    Ackerman, B.3    Bey, P.4    Pegg, A.E.5
  • 42
    • 0033634723 scopus 로고    scopus 로고
    • A cell cycle-dependent internal ribosome entry site
    • S. Pyronnet L. Pradayrol N. Sonenberg 2000 A cell cycle-dependent internal ribosome entry site Mol Cell 5 607 616
    • (2000) Mol Cell , vol.5 , pp. 607-616
    • Pyronnet, S.1    Pradayrol, L.2    Sonenberg, N.3
  • 43
    • 0027255111 scopus 로고
    • Isolation and characterization of the Drosophila ornithine decarboxylase locus: Evidence for the presence of two transcribed ODC genes in the Drosophila genome
    • E. Rom C. Kahana 1993 Isolation and characterization of the Drosophila ornithine decarboxylase locus: evidence for the presence of two transcribed ODC genes in the Drosophila genome DNA Cell Biol 12 499 508
    • (1993) DNA Cell Biol , vol.12 , pp. 499-508
    • Rom, E.1    Kahana, C.2
  • 44
    • 0032967255 scopus 로고    scopus 로고
    • Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway
    • L.M. Shantz A.E. Pegg 1999 Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway Int J Biochem Cell Biol 31 107 122
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 107-122
    • Shantz, L.M.1    Pegg, A.E.2
  • 46
    • 0027193354 scopus 로고
    • Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants
    • K.E. Tobias C. Kahana 1993 Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants Biochemistry 32 5842 5847
    • (1993) Biochemistry , vol.32 , pp. 5842-5847
    • Tobias, K.E.1    Kahana, C.2
  • 47
    • 0028509254 scopus 로고
    • TREECON for Windows: A software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment
    • Y. Van de Peer R. De Wachter 1994 TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment Comput Appl Biosci 10 569 570
    • (1994) Comput Appl Biosci , vol.10 , pp. 569-570
    • Van De Peer, Y.1    De Wachter, R.2
  • 49
    • 0034672399 scopus 로고    scopus 로고
    • A luminescence-based test for determining ornithine decarboxylase activity
    • Y. Wang U. Bachrach 2000 A luminescence-based test for determining ornithine decarboxylase activity Anal Biochem 287 299 302
    • (2000) Anal Biochem , vol.287 , pp. 299-302
    • Wang, Y.1    Bachrach, U.2
  • 50
    • 0029278912 scopus 로고
    • Molecular cloning of a bovine ornithine decarboxylase cDNA and its use in the detection of restriction fragment length polymorphisms in Holsteins
    • J. Yao D. Zadworny U. Kuhnlein J.F. Hayes 1995 Molecular cloning of a bovine ornithine decarboxylase cDNA and its use in the detection of restriction fragment length polymorphisms in Holsteins Genome 38 325 331
    • (1995) Genome , vol.38 , pp. 325-331
    • Yao, J.1    Zadworny, D.2    Kuhnlein, U.3    Hayes, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.