메뉴 건너뛰기




Volumn 11, Issue 3, 1997, Pages 429-441

Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: Cloning, expression and phylogenetic relationships

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); DICOTYLEDONEAE; ESCHERICHIA COLI; EUCALYPTUS; EUCALYPTUS GUNNII; MAMMALIA;

EID: 0031105944     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.11030429.x     Document Type: Article
Times cited : (264)

References (53)
  • 2
    • 0026521505 scopus 로고
    • Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plantdihydroflavonol reductase suparfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose 4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus
    • Baker, M.E. and Blasco, R. (1992) Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plantdihydroflavonol reductase suparfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose 4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Lett. 301, 89-93.
    • (1992) FEBS Lett. , vol.301 , pp. 89-93
    • Baker, M.E.1    Blasco, R.2
  • 3
    • 0025338352 scopus 로고
    • A common ancestor for mammalian 3β-hydroxysteroid dehydrogenase and plant dihydroflavonol reductase
    • Baker, M.E., Luu-The, V., Simard, J. and Labrie, F. (1990) A common ancestor for mammalian 3β-hydroxysteroid dehydrogenase and plant dihydroflavonol reductase. Biochem. J. 269, 558-559.
    • (1990) Biochem. J. , vol.269 , pp. 558-559
    • Baker, M.E.1    Luu-The, V.2    Simard, J.3    Labrie, F.4
  • 5
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determinated at 2.5 - Resolution
    • Bauer, A.J., Rayment, I., Frey, P.A. and Holden, H.M. (1992) The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determinated at 2.5 - resolution. Proteins, 12, 372-381.
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 6
    • 0024769577 scopus 로고
    • Flavonoid synthesis in Petunia hybrida: Partial characterization of dihydroflavonol-4-reductase genes
    • Beld, M., Martin, C., Huits, H., Stuitje, A.R. and Gerats A.G.M. (1989) Flavonoid synthesis in Petunia hybrida: partial characterization of dihydroflavonol-4-reductase genes. Plant Mol. Biol. 13, 491-502.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 491-502
    • Beld, M.1    Martin, C.2    Huits, H.3    Stuitje, A.R.4    Gerats, A.G.M.5
  • 9
    • 0023055381 scopus 로고
    • A catalogue of splice junction and putative branch point sequences from plant introns
    • Brown, J.W.S. (1986) A catalogue of splice junction and putative branch point sequences from plant introns. Nucl. Acids Res. 14, 9549-9559.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 9549-9559
    • Brown, J.W.S.1
  • 10
    • 85102330121 scopus 로고
    • Mechanistic models of forage cell wall degradation
    • (Jung, H.G., Buxton, D.R., Hatfield, R.D. and Ralph, J., eds). Madison, USA: Ann. Society of Agronomy
    • Chesson, A. (1993) Mechanistic models of forage cell wall degradation. In Forage Cell Wall Structure and Disgestibility (Jung, H.G., Buxton, D.R., Hatfield, R.D. and Ralph, J., eds). Madison, USA: Ann. Society of Agronomy, pp. 347-371
    • (1993) Forage Cell Wall Structure and Disgestibility , pp. 347-371
    • Chesson, A.1
  • 12
    • 0344735710 scopus 로고
    • Laccase and the deposition of lignin in vascular plants
    • Dean, J.F.D. and Eriksson, K.E.L. (1994) Laccase and the deposition of lignin in vascular plants. Holzforschung, 48, 21-33.
    • (1994) Holzforschung , vol.48 , pp. 21-33
    • Dean, J.F.D.1    Eriksson, K.E.L.2
  • 14
    • 0025204325 scopus 로고
    • Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene
    • Elkind, Y., Edwards, R., Mavandad, M., Hedrick, S.A., Ribak, O., Dixon, R.A. and Lamb, C.J. (1990) Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene. Proc. Natl Acad. Sci. USA, 87, 9057-9061.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9057-9061
    • Elkind, Y.1    Edwards, R.2    Mavandad, M.3    Hedrick, S.A.4    Ribak, O.5    Dixon, R.A.6    Lamb, C.J.7
  • 15
    • 0029240461 scopus 로고
    • Tissue and cell specific expression of cinnamoyl alcohol dehydogenase promoter in transgenic poplar plants
    • Feuillet, C., Lauvergeat, V., Deswarte, C., Pilate, G., Boudet A.M. and Grima-Pettenati J. (1995) Tissue and cell specific expression of cinnamoyl alcohol dehydogenase promoter in transgenic poplar plants. Plant Mol. Biol. 27, 651-667.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 651-667
    • Feuillet, C.1    Lauvergeat, V.2    Deswarte, C.3    Pilate, G.4    Boudet, A.M.5    Grima-Pettenati, J.6
  • 17
    • 0026656815 scopus 로고
    • Exhaustive matching of the entire protein sequence database
    • Gonnet, G.M., Cohen, M.A and Benner, S.A. (1992) Exhaustive matching of the entire protein sequence database. Science, 256, 1443-1445.
    • (1992) Science , vol.256 , pp. 1443-1445
    • Gonnet, G.M.1    Cohen, M.A.2    Benner, S.A.3
  • 18
    • 0027568473 scopus 로고
    • Molecular cloning and expression of a Eucalyptus gunnii cDNA clone encoding cinnamyl alcohol dehydrogenase
    • Grima-Pettenati, J., Feuillet, C., Goffner, D., Borderies, G. and Boudet, A.M. (1993) Molecular cloning and expression of a Eucalyptus gunnii cDNA clone encoding cinnamyl alcohol dehydrogenase. Plant Mol. Biol. 21, 1085-1095.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 1085-1095
    • Grima-Pettenati, J.1    Feuillet, C.2    Goffner, D.3    Borderies, G.4    Boudet, A.M.5
  • 20
    • 0031000594 scopus 로고    scopus 로고
    • Cinnamyl alcohol dehydrogenase: Identification of new sites of promoter activity in transgenic poplar
    • in press.
    • Hawkins, S.W., Samaj, J., Lauvergeat, V., Boudet, A. and Grima-Pettenati, J. (1997) Cinnamyl alcohol dehydrogenase: identification of new sites of promoter activity in transgenic poplar. Plant Physiol. in press.
    • (1997) Plant Physiol.
    • Hawkins, S.W.1    Samaj, J.2    Lauvergeat, V.3    Boudet, A.4    Grima-Pettenati, J.5
  • 21
    • 85052903690 scopus 로고
    • Biosynthesis of flavonoids
    • (Harborne, J.B., ed.). London: Chapman & Hall
    • Heller, W. and Forkmann, G. (1993) Biosynthesis of flavonoids. In The Flavonoids:Advances in Research since 1986(Harborne, J.B., ed.). London: Chapman & Hall, pp. 499-535.
    • (1993) The Flavonoids:Advances in Research since 1986 , pp. 499-535
    • Heller, W.1    Forkmann, G.2
  • 22
    • 0025896737 scopus 로고
    • Cloning, nucleotide sequence, and transcriptional analysis of the NAD(P)-dependent cholesterol dehydrogenase gene from a Nocardia sp. and its hyperexpression in Streptomyces spp
    • Horinouchi, S., Ishizuka, H. and Beppu, T. (1991) Cloning, nucleotide sequence, and transcriptional analysis of the NAD(P)-dependent cholesterol dehydrogenase gene from a Nocardia sp. and its hyperexpression in Streptomyces spp. Appl. Environ. Microbiol. 57, 1386-1393.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1386-1393
    • Horinouchi, S.1    Ishizuka, H.2    Beppu, T.3
  • 23
    • 0026486190 scopus 로고
    • Reductase activity encoded by the HM1 disease resistance gene in maize
    • Johal, G.S. and Briggs, S.P. (1992) Reductase activity encoded by the HM1 disease resistance gene in maize. Science, 258, 985-987.
    • (1992) Science , vol.258 , pp. 985-987
    • Johal, G.S.1    Briggs, S.P.2
  • 24
    • 0001515418 scopus 로고
    • High level expression of introduced chimaeric genes in regenerated transformed plants
    • Jones, J.D.G., Dunsmuir, P. and Bedbrook, J. (1985) High level expression of introduced chimaeric genes in regenerated transformed plants. EMBO J. 4, 2411-2418.
    • (1985) EMBO J. , vol.4 , pp. 2411-2418
    • Jones, J.D.G.1    Dunsmuir, P.2    Bedbrook, J.3
  • 25
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl
    • Joshi, C.P. (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl. Acids Res, 15, 6643-6653.
    • (1987) Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 26
    • 0002642606 scopus 로고
    • Cell wall lignification and degradability
    • (Jung, H.G, Buxton, D.R., Hatfieid, R.D. and Ralph, J. eds). Madison, USA: Annual Society of Agronomy
    • Jung, H.G. and Deetz, D.A. (1993) Cell wall lignification and degradability. In Forage Cell Wall Structure and Digestibility (Jung, H.G, Buxton, D.R., Hatfieid, R.D. and Ralph, J. eds). Madison, USA: Annual Society of Agronomy, pp. 315-340.
    • (1993) Forage Cell Wall Structure and Digestibility , pp. 315-340
    • Jung, H.G.1    Deetz, D.A.2
  • 27
    • 0000049761 scopus 로고
    • The possible association of phytoalexins with resistance gene expression in flax to Melampsora lini
    • Keen, N.T. and Litttefield, L.J. (1979) The possible association of phytoalexins with resistance gene expression in flax to Melampsora lini. Physiol. Plant Pathol. 14, 265-280.
    • (1979) Physiol. Plant Pathol. , vol.14 , pp. 265-280
    • Keen, N.T.1    Litttefield, L.J.2
  • 28
    • 0028155769 scopus 로고
    • The flavonoid biosynthetic pathway in plants: Function and evolution
    • Koes, R.E., Quattrocchio, F. and Mol, J.N.M. (1994) The flavonoid biosynthetic pathway in plants: function and evolution. BioEssays, 16, 123-132.
    • (1994) BioEssays , vol.16 , pp. 123-132
    • Koes, R.E.1    Quattrocchio, F.2    Mol, J.N.M.3
  • 29
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eucaryotic mRNAs
    • Kozak, M. (1984) Compilation and analysis of sequences upstream from the translational start site in eucaryotic mRNAs. Nucl. Acids Res. 12, 857-872.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (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
  • 31
    • 0001587954 scopus 로고
    • Evolution of lignan and neolignan biochemical pathways
    • (Nes, D., ed.). ACS Symposium Series No. 562. Washington, DC: American Chemical Society
    • Lewis, N.G. and Davin, L.B. (1994) Evolution of lignan and neolignan biochemical pathways. In Evolution of Natural Products (Nes, D., ed.). ACS Symposium Series No. 562. Washington, DC: American Chemical Society, pp. 202-246.
    • (1994) Evolution of Natural Products , pp. 202-246
    • Lewis, N.G.1    Davin, L.B.2
  • 32
    • 0019616796 scopus 로고
    • Enzymic synthesis of lignin precursors. Comparison of cinnamoyl-CoA reductase and cinnamyl alcohol:NADP dehydrogenase from spruce (Picea abies L.) and soybean (Glycine max L.)
    • Lüderitz, T. and Grisebach, H. (1981) Enzymic synthesis of lignin precursors. Comparison of cinnamoyl-CoA reductase and cinnamyl alcohol:NADP dehydrogenase from spruce (Picea abies L.) and soybean (Glycine max L.). Eur. J. Biochem. 119, 115-124.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 115-124
    • Lüderitz, T.1    Grisebach, H.2
  • 34
    • 0022431870 scopus 로고
    • The consensus YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3′ termini
    • MacLauchlan, J., Gaffney, D., Whitton, J.L. and Clement, J.B. (1985) The consensus YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3′ termini. Nucl. Acids Res. 13, 1347-1368.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 1347-1368
    • MacLauchlan, J.1    Gaffney, D.2    Whitton, J.L.3    Clement, J.B.4
  • 36
    • 8244251243 scopus 로고
    • Lignin characterisation in CAD down-regulated tobacco
    • 25-29 September 1995, Santiago de Compostela, Spain (Zarra, I. and Revilla, G., eds).
    • Myton, K., Stewart, D., Yahiaoui, N., McDougall, G., Marque, C. and Boudet, A.M. (1995) Lignin characterisation in CAD down-regulated tobacco. The Cell Wall Meeting CW95, 25-29 September 1995, Santiago de Compostela, Spain (Zarra, I. and Revilla, G., eds). p. 106.
    • (1995) The Cell Wall Meeting CW95 , pp. 106
    • Myton, K.1    Stewart, D.2    Yahiaoui, N.3    McDougall, G.4    Marque, C.5    Boudet, A.M.6
  • 37
    • 0001875872 scopus 로고
    • Purification, characterization and cloning of cinnamyl alcohol dehydrogenase in Loblolly Pine (Pinus taeda)
    • O'Malley, D.M., Porter, S. and Sederoff, R.R. (1992) Purification, characterization and cloning of cinnamyl alcohol dehydrogenase in Loblolly Pine (Pinus taeda). Plant Physiol. 98, 1364-1371.
    • (1992) Plant Physiol. , vol.98 , pp. 1364-1371
    • O'Malley, D.M.1    Porter, S.2    Sederoff, R.R.3
  • 38
    • 0028451105 scopus 로고
    • A cDNA encoding S-adenosyl methionine caffeic 3-O-methyltransferase from Eucalyptus
    • Poeydomenge, O., Boudet, A.M. and Grima-Pettenati, J. (1994) A cDNA encoding S-adenosyl methionine caffeic 3-O-methyltransferase from Eucalyptus. Plant Physiol. 105, 749-750.
    • (1994) Plant Physiol. , vol.105 , pp. 749-750
    • Poeydomenge, O.1    Boudet, A.M.2    Grima-Pettenati, J.3
  • 39
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost, B. and Sander, C. (1993) Prediction of protein structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 41
    • 0021402042 scopus 로고
    • Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems
    • Sarni, F., Grand, C. and Boudet, A.M. (1984) Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems. Eur. J. Biochem. 139, 259-265.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 259-265
    • Sarni, F.1    Grand, C.2    Boudet, A.M.3
  • 43
    • 0026832675 scopus 로고
    • Effects of ionizing radiation on a plant genome: Analysis of two Arabidopisis transparent testa mutations
    • Shirley, B.W., Hanley, S. and Goodman, H.M. (1992) Effects of ionizing radiation on a plant genome: analysis of two Arabidopisis transparent testa mutations. Plant Cell, 4, 333-347.
    • (1992) Plant Cell , vol.4 , pp. 333-347
    • Shirley, B.W.1    Hanley, S.2    Goodman, H.M.3
  • 44
    • 0028218683 scopus 로고
    • Modular arrangement of proteins as inferred from analysis of homology
    • Sonnhammer, E.L.L. and Kahn, D. (1994) Modular arrangement of proteins as inferred from analysis of homology. Protein Sci. 3, 482-492.
    • (1994) Protein Sci. , vol.3 , pp. 482-492
    • Sonnhammer, E.L.L.1    Kahn, D.2
  • 45
    • 0028386531 scopus 로고
    • Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L.)
    • Sparvoli, F., Martin, C., Scienza, A., Gavazzi, G. and Tonelli, C. (1994) Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L.). Plant Mol. Biol. 24, 743-755.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 743-755
    • Sparvoli, F.1    Martin, C.2    Scienza, A.3    Gavazzi, G.4    Tonelli, C.5
  • 46
    • 0001477970 scopus 로고
    • Flavonoid evolution: An enzymic approach
    • Stafford, H. (1991) Flavonoid evolution: an enzymic approach. Plant Physiol. 96, 680-685.
    • (1991) Plant Physiol. , vol.96 , pp. 680-685
    • Stafford, H.1
  • 47
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S. and Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl Acad. Sci. USA, 82, 1074-1078.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 48
    • 0001596403 scopus 로고
    • Activity and accumulation of cell division-promoting phenolics in tobacco tissue cultures
    • Teutonico, R.A., Dudley, M.W., Orr, J.D., Lynn, D.G. and Binns, A.N. (1991) Activity and accumulation of cell division-promoting phenolics in tobacco tissue cultures. Plant Physiol. 97, 288-297.
    • (1991) Plant Physiol. , vol.97 , pp. 288-297
    • Teutonico, R.A.1    Dudley, M.W.2    Orr, J.D.3    Lynn, D.G.4    Binns, A.N.5
  • 49
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 0000132949 scopus 로고
    • Regulation of lignification in defense
    • (Boller, T. and Meins, F., eds). Vienna: Springer
    • Walter, M.H. (1992) Regulation of lignification in defense. In Plant Gene Research. Genes Involved in Plant Defense (Boller, T. and Meins, F., eds). Vienna: Springer, pp. 327-352.
    • (1992) Plant Gene Research. Genes Involved in Plant Defense , pp. 327-352
    • Walter, M.H.1
  • 51
    • 0017111631 scopus 로고
    • Enzymic synthesis of lignin precursors: Purification and properties of a cinnamoyl-CoA:NADPH reductase from cell suspension cultures of soybean (Glycine max. L.)
    • Wegenmayer, H., Ebel, J. and Grisebach, H. (1976) Enzymic synthesis of lignin precursors: Purification and properties of a cinnamoyl-CoA:NADPH reductase from cell suspension cultures of soybean (Glycine max. L.). Eur. J. Biochem. 65, 529-536.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 529-536
    • Wegenmayer, H.1    Ebel, J.2    Grisebach, H.3
  • 52
    • 0029360329 scopus 로고
    • The formation of mRNA 3′-ends in plants
    • Wu, L., Ueda, T. and Messing, J. (1995) The formation of mRNA 3′-ends in plants. Plant J. 8, 323-329.
    • (1995) Plant J. , vol.8 , pp. 323-329
    • Wu, L.1    Ueda, T.2    Messing, J.3
  • 53
    • 0025685419 scopus 로고
    • Structure and sexual dimorphic expression of a liver-specific rat 3β-hydroxysteroid dehydrogenase/isomerase
    • Zhao, H.F., Rheaume, E., Trudel, C., Couet, J., Labrie, F. and Simard, J. (1990) Structure and sexual dimorphic expression of a liver-specific rat 3β-hydroxysteroid dehydrogenase/isomerase. Endocrinology, 127, 3237-3239.
    • (1990) Endocrinology , vol.127 , pp. 3237-3239
    • Zhao, H.F.1    Rheaume, E.2    Trudel, C.3    Couet, J.4    Labrie, F.5    Simard, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.