메뉴 건너뛰기




Volumn 40, Issue 1, 1999, Pages 121-131

Analysis of promoters from tyrosine/dihydroxyphenylalanine decarboxylase and berberine bridge enzyme genes involved in benzylisoquinoline alkaloid biosynthesis in opium poppy

Author keywords

Benzylisoquinoline alkaloids; Berberine bridge enzyme; Molecular regulation; Opium poppy; Papaver somniferum; Secondary metabolism; Tyrosine dihydroxyphenylalanine decarboxylase

Indexed keywords

AROMATIC LEVO AMINO ACID DECARBOXYLASE; BENZYLISOQUINOLINE ALKALOID; BERBERINE BRIDGE ENZYME; BETA GLUCURONIDASE; BIOCHEMICAL PATHWAY; BIOSYNTHESIS; CLONE; DELETION MUTAGENESIS; DNA FLANKING REGION; ENZYME ACTIVITY; GENE INDUCTION; MESSENGER RNA; MICROPROJECTILE BOMBARDMENT; PLANT CELL CULTURE; PROMOTER REGION; REPORTER GENE; RNA ANALYSIS; TYROSINE DECARBOXYLASE; WOUND;

EID: 0033136796     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026433112119     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0000669341 scopus 로고
    • Two methylenedioxy bridge forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis
    • Bauer, W. and Zenk, M.H. 1991. Two methylenedioxy bridge forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30: 2953-2961.
    • (1991) Phytochemistry , vol.30 , pp. 2953-2961
    • Bauer, W.1    Zenk, M.H.2
  • 3
    • 0026655058 scopus 로고
    • Strictosidine synthase from Rauwolfia serpentina: Analysis of a gene involved in indole alkaloid biosynthesis
    • Bracher, D. and Kutchan, T.M. 1992. Strictosidine synthase from Rauwolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis. Arch. Biochem. Biophys. 294: 717-723.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 717-723
    • Bracher, D.1    Kutchan, T.M.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000867274 scopus 로고
    • Stimulation of sanguinarine production by combined fungal elicitation and hormonal deprivation in cell suspension cultures of Papaver bracteatum
    • Cline, S.D. and Coscia, C.J. 1988. Stimulation of sanguinarine production by combined fungal elicitation and hormonal deprivation in cell suspension cultures of Papaver bracteatum. Plant Physiol. 86: 161-165.
    • (1988) Plant Physiol. , vol.86 , pp. 161-165
    • Cline, S.D.1    Coscia, C.J.2
  • 6
    • 0023605130 scopus 로고
    • Mapping of gene transcripts by nuclease protection assays and cDNA primer extension
    • Calzone, F.J., Britten, R.J. and Davidson, E.H. 1987. Mapping of gene transcripts by nuclease protection assays and cDNA primer extension. Meth. Enzymol. 152: 611-632.
    • (1987) Meth. Enzymol. , vol.152 , pp. 611-632
    • Calzone, F.J.1    Britten, R.J.2    Davidson, E.H.3
  • 8
    • 0025751609 scopus 로고
    • Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack
    • Dittrich, H. and Kutchan, T.M. 1991. Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. USA 88: 9969-9973.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9969-9973
    • Dittrich, H.1    Kutchan, T.M.2
  • 9
    • 0028829961 scopus 로고
    • Stress-induced phenylpropanoid metabolism
    • Dixon, R.A. and Paiva, N.L. 1995. Stress-induced phenylpropanoid metabolism. Plant Cell 7: 1085-1097.
    • (1995) Plant Cell , vol.7 , pp. 1085-1097
    • Dixon, R.A.1    Paiva, N.L.2
  • 10
    • 0021909905 scopus 로고
    • Comparative in vivo activity of sanguinarine against oral microbial isolates
    • Dzink, J.L. and Socransky, S.S. 1985. Comparative in vivo activity of sanguinarine against oral microbial isolates. Antimicrob. Agents Chemother. 27: 663-665.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 663-665
    • Dzink, J.L.1    Socransky, S.S.2
  • 11
    • 0002555072 scopus 로고
    • Stimulation of sanguinarine accumulation in Papaver somniferum cell cultures by fungal elicitors
    • Eilert, U., Kurz, W.G.W, and Constabel, F. 1985. Stimulation of sanguinarine accumulation in Papaver somniferum cell cultures by fungal elicitors. J. Plant Physiol. 119: 65-76.
    • (1985) J. Plant Physiol. , vol.119 , pp. 65-76
    • Eilert, U.1    Kurz, W.G.W.2    Constabel, F.3
  • 12
    • 0028125304 scopus 로고
    • Differential and tissue-specific expression of a gene family for tyrosine/dopa decarboxylase in opium poppy
    • Facchini, P.J. and De Luca, V. 1994. Differential and tissue-specific expression of a gene family for tyrosine/dopa decarboxylase in opium poppy. J. Biol. Chem. 269: 26684-26690.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26684-26690
    • Facchini, P.J.1    De Luca, V.2
  • 13
    • 0029201588 scopus 로고
    • Phloem-specific expression of tyrosine/dopa decarboxylase genes and the biosynthesis of isoquinoline alkaloids in opium poppy
    • Facchini, P.J. and De Luca, V. 1995. Phloem-specific expression of tyrosine/dopa decarboxylase genes and the biosynthesis of isoquinoline alkaloids in opium poppy. Plant Cell 7: 1811-1821.
    • (1995) Plant Cell , vol.7 , pp. 1811-1821
    • Facchini, P.J.1    De Luca, V.2
  • 14
    • 0030194513 scopus 로고    scopus 로고
    • Uncoupled defense gene expression and antimicrobial alkaloid accumulation in elicited opium poppy cell cultures
    • Facchini, P.J., Johnson, A.G., Poupart, J. and De Luca, V. 1996a. Uncoupled defense gene expression and antimicrobial alkaloid accumulation in elicited opium poppy cell cultures. Plant Physiol. 111: 687-697.
    • (1996) Plant Physiol. , vol.111 , pp. 687-697
    • Facchini, P.J.1    Johnson, A.G.2    Poupart, J.3    De Luca, V.4
  • 15
    • 0030468681 scopus 로고    scopus 로고
    • Molecular characterization of berberine bridge enzyme genes from opium poppy
    • Facchini, P.J., Penzes, C., Johnson, A.G. and Bull, D. 1996b. Molecular characterization of berberine bridge enzyme genes from opium poppy. Plant Physiol. 112: 1669-1677.
    • (1996) Plant Physiol. , vol.112 , pp. 1669-1677
    • Facchini, P.J.1    Penzes, C.2    Johnson, A.G.3    Bull, D.4
  • 16
    • 0032160760 scopus 로고    scopus 로고
    • Expression patterns conferred by tyrosine/dihydroxyphenylalanine decarboxylase promoters from opium poppy are conserved in transgenic tobacco
    • Facchini, P.J., Penzes-Yost, C., Samanani, N. and Kowalchuk, B. 1998. Expression patterns conferred by tyrosine/dihydroxyphenylalanine decarboxylase promoters from opium poppy are conserved in transgenic tobacco. Plant Physiol. 118: 69-81.
    • (1998) Plant Physiol. , vol.118 , pp. 69-81
    • Facchini, P.J.1    Penzes-Yost, C.2    Samanani, N.3    Kowalchuk, B.4
  • 17
    • 0021381028 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments for high specific activity
    • Feinberg, A.P. and Vogelstein, B. 1984. A technique for radiolabeling DNA restriction endonuclease fragments for high specific activity. Anal. Biochem. 137: 266-269.
    • (1984) Anal. Biochem. , vol.137 , pp. 266-269
    • Feinberg, A.P.1    Vogelstein, B.2
  • 18
    • 0008303594 scopus 로고
    • Stereochemistry of enzymatic formation of the berberine bridge in protoberberine alkaloids
    • Frenzel, T., Beale, J.M., Kobayashi, M., Zenk, M.H. and Floss, H.G. 1988. Stereochemistry of enzymatic formation of the berberine bridge in protoberberine alkaloids. J. Am. Chem. Soc. 110: 7878-7880.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7878-7880
    • Frenzel, T.1    Beale, J.M.2    Kobayashi, M.3    Zenk, M.H.4    Floss, H.G.5
  • 19
    • 0001267967 scopus 로고
    • S-Adenosyl-L-methionine: 3′-hydroxy-N-methyl-(S)-coclaurine-4′-O-methyltransferase, a regio- and stereoselective enzyme of the (S)-reticuline pathway
    • 1990
    • Frenzel, T. and Zenk, M.H. 1990. S-Adenosyl-L-methionine: 3′-hydroxy-N-methyl-(S)-coclaurine-4′-O-methyltransferase, a regio- and stereoselective enzyme of the (S)-reticuline pathway. Phytochemistry 29: 3505-3511 (1990).
    • (1990) Phytochemistry , vol.29 , pp. 3505-3511
    • Frenzel, T.1    Zenk, M.H.2
  • 20
    • 0014276538 scopus 로고
    • Nutrient requirements of suspension cultures of soybean root cells
    • Gamborg, O.L., Miller, R.O. and Ojima, K. 1968. Nutrient requirements of suspension cultures of soybean root cells. Exp. Cell Res. 50: 151-158.
    • (1968) Exp. Cell Res. , vol.50 , pp. 151-158
    • Gamborg, O.L.1    Miller, R.O.2    Ojima, K.3
  • 21
    • 0032005070 scopus 로고    scopus 로고
    • Isolation and analysis of a gene bbel encoding the berberine bridge enzyme from the California poppy Eschscholzia californica
    • Hauschild K., Pauli H.H., Kutchan, T.M. 1998. Isolation and analysis of a gene bbel encoding the berberine bridge enzyme from the California poppy Eschscholzia californica. Plant Mol. Biol. 36: 473-478.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 473-478
    • Hauschild, K.1    Pauli, H.H.2    Kutchan, T.M.3
  • 22
    • 0028814339 scopus 로고
    • Genetics and biochemistry of anthocyanin biosynthesis
    • Holton, T.A. and Cornish, B.C. 1995. Genetics and biochemistry of anthocyanin biosynthesis. Plant Cell 7: 1071-1083.
    • (1995) Plant Cell , vol.7 , pp. 1071-1083
    • Holton, T.A.1    Cornish, B.C.2
  • 23
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R.A., Kavanagh, T.A. and Bevan, M.W. 1987. GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6: 3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 24
    • 77956684330 scopus 로고
    • Molecular genetics of plant alkaloid biosynthesis
    • G. Cordell (Ed.), Academic Press, San Diego
    • Kutchan, T.M. 1988. Molecular genetics of plant alkaloid biosynthesis. In: G. Cordell (Ed.), The Alkaloids, vol. 50, Academic Press, San Diego, pp. 257-316.
    • (1988) The Alkaloids , vol.50 , pp. 257-316
    • Kutchan, T.M.1
  • 25
    • 0028874083 scopus 로고
    • Alkaloid biosynthesis: The basis for metabolic engineering of medicinal plants
    • Kutchan, T.M. 1995. Alkaloid biosynthesis: the basis for metabolic engineering of medicinal plants. Plant Cell 7: 1059-1070.
    • (1995) Plant Cell , vol.7 , pp. 1059-1070
    • Kutchan, T.M.1
  • 26
    • 0023654956 scopus 로고
    • Improved method for the isolation of RNA from plant tissues
    • Logemann, J., Schell, J. and Willmitzer, L. 1987. Improved method for the isolation of RNA from plant tissues. Anal. Biochem. 163: 16-20.
    • (1987) Anal. Biochem. , vol.163 , pp. 16-20
    • Logemann, J.1    Schell, J.2    Willmitzer, L.3
  • 27
    • 0001781047 scopus 로고
    • Elicitor-induced L-tyrosine decarboxylase from plant cell suspension cultures. I. Induction and purification
    • Marques, I.A. and Brodelius, P.E. 1988. Elicitor-induced L-tyrosine decarboxylase from plant cell suspension cultures. I. Induction and purification. Plant Physiol. 88: 47-51.
    • (1988) Plant Physiol. , vol.88 , pp. 47-51
    • Marques, I.A.1    Brodelius, P.E.2
  • 28
    • 0025389213 scopus 로고
    • In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene
    • McKendree, W.L., Paul, A.-L., DeLisle, A.J. and Ferl, R.J. 1990. In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene. Plant Cell 2: 207-214.
    • (1990) Plant Cell , vol.2 , pp. 207-214
    • McKendree, W.L.1    Paul, A.-L.2    DeLisle, A.J.3    Ferl, R.J.4
  • 29
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray, M. and Thompson, W.F. 1990. Rapid isolation of high molecular weight plant DNA. Nucl. Acids Res. 8: 4321-4325.
    • (1990) Nucl. Acids Res. , vol.8 , pp. 4321-4325
    • Murray, M.1    Thompson, W.F.2
  • 30
    • 0000494576 scopus 로고
    • Cell wall perforations in laticifers of Papaver somniferum L.
    • Nessler, C.L. and Mahlberg, P.G. 1977. Cell wall perforations in laticifers of Papaver somniferum L. Bot. Gaz. 138: 402-408.
    • (1977) Bot. Gaz. , vol.138 , pp. 402-408
    • Nessler, C.L.1    Mahlberg, P.G.2
  • 31
    • 0001078184 scopus 로고
    • Ontogeny and cytochemistry of alkaloid vesicles in laticifers of Papaver somniferum L
    • Nessler, C.L. and Mahlberg, P.G. 1978. Ontogeny and cytochemistry of alkaloid vesicles in laticifers of Papaver somniferum L. Am. J. Bot. 64: 541-551.
    • (1978) Am. J. Bot. , vol.64 , pp. 541-551
    • Nessler, C.L.1    Mahlberg, P.G.2
  • 32
    • 0000982778 scopus 로고
    • Distant precursors of benzylisoquinoline alkaloids and their enzymatic formation
    • Rueffer, M. and Zenk, M.H. 1987. Distant precursors of benzylisoquinoline alkaloids and their enzymatic formation. Z. Naturforsch. 42C: 319-332.
    • (1987) Z. Naturforsch. , vol.42 C , pp. 319-332
    • Rueffer, M.1    Zenk, M.H.2
  • 35
    • 0024689740 scopus 로고
    • Functional architecture of the light-responsive chalcone synthase promoter from parsley
    • Schulze-Lefert, P., Becker-André, M., Schulz, W., Hahlbrock, K. and Dangl, J.L. 1989. Functional architecture of the light-responsive chalcone synthase promoter from parsley. Plant Cell 1: 707-714.
    • (1989) Plant Cell , vol.1 , pp. 707-714
    • Schulze-Lefert, P.1    Becker-André, M.2    Schulz, W.3    Hahlbrock, K.4    Dangl, J.L.5
  • 36
    • 0001598073 scopus 로고
    • Elicitation of benzophenanthridine alkaloid biosynthesis in Eschscholtzia cell cultures
    • Schumacher, H.-M., Gundlach, H., Fiedler, F. and Zenk, M.H. 1987. Elicitation of benzophenanthridine alkaloid biosynthesis in Eschscholtzia cell cultures. Plant Cell Rep. 6: 410-413.
    • (1987) Plant Cell Rep. , vol.6 , pp. 410-413
    • Schumacher, H.-M.1    Gundlach, H.2    Fiedler, F.3    Zenk, M.H.4
  • 38
    • 0001322468 scopus 로고
    • Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis
    • Stadler, R., Kutchan, T.M. and Zenk, M.H. 1989. Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis. Phytochemistry 28: 1083-1086.
    • (1989) Phytochemistry , vol.28 , pp. 1083-1086
    • Stadler, R.1    Kutchan, T.M.2    Zenk, M.H.3
  • 39
    • 0024730591 scopus 로고
    • A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein
    • Staiger, D., Kaulen, H. and Schell, J. 1989. A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proc. Natl. Acad. Sci. USA 86: 6930-6934.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6930-6934
    • Staiger, D.1    Kaulen, H.2    Schell, J.3
  • 40
    • 0000760039 scopus 로고
    • Purification and characterization of the berberine bridge enzyme from Berberis beaniana cell cultures
    • Steffens, P., Nagakura, N. and Zenk, M.H. 1985. Purification and characterization of the berberine bridge enzyme from Berberis beaniana cell cultures. Phytochemistry 24: 2577-2583.
    • (1985) Phytochemistry , vol.24 , pp. 2577-2583
    • Steffens, P.1    Nagakura, N.2    Zenk, M.H.3
  • 41
    • 0000860639 scopus 로고
    • Elicitor induction and characterization of microsomal protopine-6-hydroxylase, the central enzyme in benzophenanthridine alkaloid biosynthesis
    • Tanahashi, T. and Zenk, M.H. 1990. Elicitor induction and characterization of microsomal protopine-6-hydroxylase, the central enzyme in benzophenanthridine alkaloid biosynthesis. Phytochemistry 29: 1113-1122.
    • (1990) Phytochemistry , vol.29 , pp. 1113-1122
    • Tanahashi, T.1    Zenk, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.