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Volumn 4, Issue , 2004, Pages

Molecular cloning and functional expression of geranylgeranyl pyrophosphate synthase from Coleus forskohlii Briq

Author keywords

[No Author keywords available]

Indexed keywords

COLEUS; ERWINIA; ESCHERICHIA COLI; NICOTIANA TABACUM; PANTOEA ANANATIS; PLECTRANTHUS BARBATUS;

EID: 12344252035     PISSN: 14712229     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-4-18     Document Type: Article
Times cited : (48)

References (31)
  • 1
  • 2
    • 0019358486 scopus 로고
    • The positive inotropic-acting forskolin, a potent adenylatecyclase activator
    • Metzger H, Lindner E: The positive inotropic-acting forskolin, a potent adenylatecyclase activator. Drug Res 1981, 31:1248-1250.
    • (1981) Drug Res , vol.31 , pp. 1248-1250
    • Metzger, H.1    Lindner, E.2
  • 6
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer M, Knani M, Simonin P, Sutter B, Sahm H: Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem J 1993, 295:517-524.
    • (1993) Biochem J , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 7
    • 0029922877 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis
    • Rohmer M, Seemann M, Horbach S, Bringer-Meyer S, Sahm K: Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis. J Am Chem Soc 1996, 118:2564-2566.
    • (1996) J Am Chem Soc , vol.118 , pp. 2564-2566
    • Rohmer, M.1    Seemann, M.2    Horbach, S.3    Bringer-Meyer, S.4    Sahm, K.5
  • 8
    • 0033229957 scopus 로고    scopus 로고
    • Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution
    • Wang K, Ohnuma S: Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution. Trends Biochem Sci 1999, 24:445-451.
    • (1999) Trends Biochem Sci , vol.24 , pp. 445-451
    • Wang, K.1    Ohnuma, S.2
  • 9
    • 0034002980 scopus 로고    scopus 로고
    • Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis
    • Okada K, Saito T, Nakagawa T, Kawamukai M, Kamiya Y: Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis. Plant Physiol 2000, 122:1045-1056.
    • (2000) Plant Physiol , vol.122 , pp. 1045-1056
    • Okada, K.1    Saito, T.2    Nakagawa, T.3    Kawamukai, M.4    Kamiya, Y.5
  • 10
    • 0031105491 scopus 로고    scopus 로고
    • Cloning and functional expression of a novel geranylgeranyl pyrophosphate synthase gene from Arabidopsis thaliana in Escherichia coli
    • Zhu XF, Suzuki K, Okada K, Tanaka K, Nakagawa T, Kawamukai M, Matsuda K: Cloning and functional expression of a novel geranylgeranyl pyrophosphate synthase gene from Arabidopsis thaliana in Escherichia coli. Plant Cell Physiol 1997, 38:357-361.
    • (1997) Plant Cell Physiol , vol.38 , pp. 357-361
    • Zhu, X.F.1    Suzuki, K.2    Okada, K.3    Tanaka, K.4    Nakagawa, T.5    Kawamukai, M.6    Matsuda, K.7
  • 11
    • 0032422236 scopus 로고    scopus 로고
    • Cloning and functional expression of a cDNA encoding geranylgeranyl diphosphate synthase from Taxus canadensis and assessment of the role of this prenyltransferase in cells induced for taxol production
    • Hefner J, Ketchum FEB, Croteau R: Cloning and functional expression of a cDNA encoding geranylgeranyl diphosphate synthase from Taxus canadensis and assessment of the role of this prenyltransferase in cells induced for taxol production. Arch Biochem Biophys 1998, 360:62-74.
    • (1998) Arch Biochem Biophys , vol.360 , pp. 62-74
    • Hefner, J.1    Ketchum, F.E.B.2    Croteau, R.3
  • 12
    • 0033673119 scopus 로고    scopus 로고
    • Cloning, characterization, and heterologous expression of a functional geranylgeranyl pyrophosphate synthase from sunflower (Helianthus annuus L.)
    • Oh SK, Kim IJ, Shin DH, Yang J, Kang H, Han KH: Cloning, characterization, and heterologous expression of a functional geranylgeranyl pyrophosphate synthase from sunflower (Helianthus annuus L.). J Plant Physiol 2000, 157:535-542.
    • (2000) J Plant Physiol , vol.157 , pp. 535-542
    • Oh, S.K.1    Kim, I.J.2    Shin, D.H.3    Yang, J.4    Kang, H.5    Han, K.H.6
  • 13
    • 0035117266 scopus 로고    scopus 로고
    • Geranylgeranyl diphosphate synthase from Scoparia dulcis and Croton sublyratus. Plastid localization and conversion to a farnesyl diphosphate synthase by mutagenesis
    • Sitthithaworn W, Kojima N, Viroonchatapan E, Suh DY, Iwanami N, Hayashi T, Noji M, Saito K, Niwa Y, Sankawa U: Geranylgeranyl diphosphate synthase from Scoparia dulcis and Croton sublyratus. Plastid localization and conversion to a farnesyl diphosphate synthase by mutagenesis. Chem Pharm Bull 2001, 49:197-202.
    • (2001) Chem Pharm Bull , vol.49 , pp. 197-202
    • Sitthithaworn, W.1    Kojima, N.2    Viroonchatapan, E.3    Suh, D.Y.4    Iwanami, N.5    Hayashi, T.6    Noji, M.7    Saito, K.8    Niwa, Y.9    Sankawa, U.10
  • 14
    • 0028283930 scopus 로고
    • Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase
    • Ohnuma S, Suzuki M, Nishino T: Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase. J Biol Chem 1994, 269:14792-14797.
    • (1994) J Biol Chem , vol.269 , pp. 14792-14797
    • Ohnuma, S.1    Suzuki, M.2    Nishino, T.3
  • 15
    • 0027233073 scopus 로고
    • Functional identification of al-3 from Neurospora crassa as the gene for geranylgeranyl pyrophosphate synthase by complementation with crt genes, in vitro characterization of the gene product and mutant analysis
    • Sandmann G, Misawa N, Wiedemann M, Vittorioso P, Carattoli A, Morelli G, Macino G: Functional identification of al-3 from Neurospora crassa as the gene for geranylgeranyl pyrophosphate synthase by complementation with crt genes, in vitro characterization of the gene product and mutant analysis. J Photochem Photobiol B: Biol 1993, 18:245-251.
    • (1993) J Photochem Photobiol B: Biol , vol.18 , pp. 245-251
    • Sandmann, G.1    Misawa, N.2    Wiedemann, M.3    Vittorioso, P.4    Carattoli, A.5    Morelli, G.6    Macino, G.7
  • 16
    • 0033602433 scopus 로고    scopus 로고
    • Identification of the GGPSI genes encoding geranylgeranyl diphosphate synthases from mouse and human
    • Kainou T, Kawamura K, Tanaka K, Matsuda H, Kawamukai M: Identification of the GGPS1 genes encoding geranylgeranyl diphosphate synthases from mouse and human. Biochim Biophys Acta 1999, 1437:333-340.
    • (1999) Biochim Biophys Acta , vol.1437 , pp. 333-340
    • Kainou, T.1    Kawamura, K.2    Tanaka, K.3    Matsuda, H.4    Kawamukai, M.5
  • 17
    • 0029155977 scopus 로고
    • Molecular cloning and nucleotide sequences of the genes for two essential proteins constituting a novel enzyme for heptaprenyl diphosphate synthesis
    • Koike-Takeshita A, Koyama T, Obata S, Ogura K: Molecular cloning and nucleotide sequences of the genes for two essential proteins constituting a novel enzyme for heptaprenyl diphosphate synthesis. J Biol Chem 1995, 270:18396-18400.
    • (1995) J Biol Chem , vol.270 , pp. 18396-18400
    • Koike-Takeshita, A.1    Koyama, T.2    Obata, S.3    Ogura, K.4
  • 18
    • 0029785708 scopus 로고    scopus 로고
    • Conversion of product specificity of archaebacterial geranylgeranyl- diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction
    • Ohnuma S, Hirooka K, Hemmi H, Ishida C, Ohto C, Nishino T: Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction. J Biol Chem 1996, 271:18831-18837.
    • (1996) J Biol Chem , vol.271 , pp. 18831-18837
    • Ohnuma, S.1    Hirooka, K.2    Hemmi, H.3    Ishida, C.4    Ohto, C.5    Nishino, T.6
  • 19
    • 0025630190 scopus 로고
    • Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli
    • Misawa N, Nakagawa M, Kobayashi K, Yamano S, Izawa Y, Nakamura K, Harashima K: Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli. J Bacteriol 1990, 172:6704-6712.
    • (1990) J Bacteriol , vol.172 , pp. 6704-6712
    • Misawa, N.1    Nakagawa, M.2    Kobayashi, K.3    Yamano, S.4    Izawa, Y.5    Nakamura, K.6    Harashima, K.7
  • 20
    • 0026731820 scopus 로고
    • COQ2 is a candidate for the structural gene encoding parahydroxybenzoate: Polyprenyl-transferase
    • Ashby MN, Kutsunai SY, Ackerman S, Tzagoloff A, Edwards PA: COQ2 is a candidate for the structural gene encoding parahydroxybenzoate: polyprenyl-transferase. J Biol Chem 1992, 267:4128-4136.
    • (1992) J Biol Chem , vol.267 , pp. 4128-4136
    • Ashby, M.N.1    Kutsunai, S.Y.2    Ackerman, S.3    Tzagoloff, A.4    Edwards, P.A.5
  • 21
    • 0027768770 scopus 로고
    • Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity
    • Joly A, Edward PA: Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity. J Biol Chem 1993, 268:26983-26989.
    • (1993) J Biol Chem , vol.268 , pp. 26983-26989
    • Joly, A.1    Edward, P.A.2
  • 22
    • 0028288134 scopus 로고
    • Yeast farnesyl-diphosphate synthase: Site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II
    • Song L, Poulter CD: Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc Natl Acad Sci USA 1994, 91:3044-3048.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3044-3048
    • Song, L.1    Poulter, C.D.2
  • 23
    • 0026618026 scopus 로고
    • Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: Correlative increase in enzyme activity and transcript level during fruit ripening
    • Kuntz M, Romer S, Suire C, Hugueney P, Weil JH, Schantz R, Carmara B: Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening. Plant J 1992, 2:25-34.
    • (1992) Plant J , vol.2 , pp. 25-34
    • Kuntz, M.1    Romer, S.2    Suire, C.3    Hugueney, P.4    Weil, J.H.5    Schantz, R.6    Carmara, B.7
  • 24
    • 0029897010 scopus 로고    scopus 로고
    • Rapid analysis of small samples containing forskolin using monoclonal antibodies
    • Yanagihara H, Sakata R, Shoyama Y, Murakami H: Rapid analysis of small samples containing forskolin using monoclonal antibodies. Planta Med 1996, 62:169-172.
    • (1996) Planta Med , vol.62 , pp. 169-172
    • Yanagihara, H.1    Sakata, R.2    Shoyama, Y.3    Murakami, H.4
  • 26
    • 21444442211 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of recombinant 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Coleus forskohlii Briq
    • in press
    • Engprasert S, Taura F, Shoyama Y: Molecular cloning, expression and characterization of recombinant 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Coleus forskohlii Briq. Plant Science in press.
    • Plant Science
    • Engprasert, S.1    Taura, F.2    Shoyama, Y.3
  • 27
    • 0026568783 scopus 로고
    • Tobacco BY-2 cell line as the "Hela" cell in the cell biology of higher plants
    • Natakata T, Nemoto Y, Hasezawa S: Tobacco BY-2 cell line as the "Hela" cell in the cell biology of higher plants. Int Rev Cytol 1992, 132:1-30.
    • (1992) Int Rev Cytol , vol.132 , pp. 1-30
    • Natakata, T.1    Nemoto, Y.2    Hasezawa, S.3
  • 28
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987, 162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 29
    • 0033136084 scopus 로고    scopus 로고
    • Non-invasive quantivative detection and applications of non-toxic, S56T-type green fluorescent protein in living plants
    • Niwa Y, Hirano T, Yoshimoto K, Shimizu M, Kobayashi H: Non-invasive quantivative detection and applications of non-toxic, S56T-type green fluorescent protein in living plants. Plant J 1999, 18:455-463.
    • (1999) Plant J , vol.18 , pp. 455-463
    • Niwa, Y.1    Hirano, T.2    Yoshimoto, K.3    Shimizu, M.4    Kobayashi, H.5
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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