메뉴 건너뛰기




Volumn 12, Issue 1, 1997, Pages 169-178

Yeast 5-aminolevulinate synthase provides additional chlorophyll precursor in transgenic tobacco

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; NICOTIANA OBTUSIFOLIA; NICOTIANA TABACUM; SACCHAROMYCES CEREVISIAE;

EID: 0031194480     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.12010169.x     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0024369147 scopus 로고
    • Distribution of the δ-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups
    • Avissar, Y., Ormerod, J.G. and Beale, S.I. (1989) Distribution of the δ-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups. Arch. Microbiol. 151, 513-519.
    • (1989) Arch. Microbiol. , vol.151 , pp. 513-519
    • Avissar, Y.1    Ormerod, J.G.2    Beale, S.I.3
  • 2
    • 0002383191 scopus 로고
    • Tetrapyrrole metabolism in photosynthetic organisms
    • Dailey H.A., ed. New York: McGraw Hill
    • Beale, S.I. and Weinstein, J.D. (1990) Tetrapyrrole metabolism in photosynthetic organisms. In Biosynthesis of Heme and Chlorophyll (Dailey H.A., ed.). New York: McGraw Hill, pp. 287-391.
    • (1990) Biosynthesis of Heme and Chlorophyll , pp. 287-391
    • Beale, S.I.1    Weinstein, J.D.2
  • 3
    • 0025098346 scopus 로고
    • Binary vectors which allow the exchange of plant selectable markers and reporter genes
    • Becker, D. (1990) Binary vectors which allow the exchange of plant selectable markers and reporter genes. Nucl. Acids Res. 18, 203.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 203
    • Becker, D.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000320052 scopus 로고
    • Synthesis of the aspartate family and branched-chain amino acids
    • Miflin, B.J., ed. Academic Press Inc.
    • Bryan, J.K. (1980) Synthesis of the aspartate family and branched-chain amino acids. In The Biochemistry of Plants Volume 5, (Miflin, B.J., ed.). Academic Press Inc., pp. 403-452
    • (1980) The Biochemistry of Plants , vol.5 , pp. 403-452
    • Bryan, J.K.1
  • 6
    • 0030087937 scopus 로고    scopus 로고
    • Mitochondrial and chloroplast targeting sequences in tandem modify protein import specificity in plant organelles
    • Castro Silva Filho, de M., Chaumont, F., Leterme, S. and Boutry, M. (1996) Mitochondrial and chloroplast targeting sequences in tandem modify protein import specificity in plant organelles. Plant Mol. Biol. 30, 769-780.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 769-780
    • Castro Silva Filho, D.M.1    Chaumont, F.2    Leterme, S.3    Boutry, M.4
  • 7
    • 0028518930 scopus 로고
    • Biosynthesis of lysine in plants: The putative role of meso-diaminopimelate dehydrogenase
    • Chatterjee, S.P., Singh, B.K. and Gilvarg, C. (1994) Biosynthesis of lysine in plants: the putative role of meso-diaminopimelate dehydrogenase. Plant Mol. Biol. 26, 285-290.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 285-290
    • Chatterjee, S.P.1    Singh, B.K.2    Gilvarg, C.3
  • 8
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczinsky, P. and Sacchi, N. (1987) Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczinsky, P.1    Sacchi, N.2
  • 9
    • 0027446537 scopus 로고
    • Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium
    • Elliot, T. (1993) Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium. J. Bacteriol. 175, 325-331
    • (1993) J. Bacteriol. , vol.175 , pp. 325-331
    • Elliot, T.1
  • 10
    • 0029027246 scopus 로고
    • 5-aminolevulinate synthase and first step of heme biosynthesis
    • Ferreira, G.C. and Gong, J. (1995) 5-aminolevulinate synthase and first step of heme biosynthesis. J. Bioenerg Biomembr. 27, 151-159.
    • (1995) J. Bioenerg Biomembr. , vol.27 , pp. 151-159
    • Ferreira, G.C.1    Gong, J.2
  • 11
    • 0000955919 scopus 로고
    • Gabaculine inhibits δ-ALA synthesis in chloroplasts
    • Flint, D.H. (1984) Gabaculine inhibits δ-ALA synthesis in chloroplasts. Plant Physiol. 75, Supp., p. 170.
    • (1984) Plant Physiol. , vol.75 , Issue.SUPPL. , pp. 170
    • Flint, D.H.1
  • 12
    • 84874757898 scopus 로고
    • Initial stages in the biosynthesis of porphyrins II. The formation of 5-aminolevulinic acid from glycine and succinyl-CoA by particles from chicken erythrocytes
    • Gibson, K.D., Laver, W.G. and Neuberger, A. (1958) Initial stages in the biosynthesis of porphyrins II. The formation of 5-aminolevulinic acid from glycine and succinyl-CoA by particles from chicken erythrocytes. Biochem. J. 61, 618-629.
    • (1958) Biochem. J. , vol.61 , pp. 618-629
    • Gibson, K.D.1    Laver, W.G.2    Neuberger, A.3
  • 13
    • 0344891524 scopus 로고    scopus 로고
    • Restriction of chlorophyll synthesis due to expression of glutamate 1-semialdehyde aminotransferase antisense RNA does not reduce the light-harvesting antenna size in tobacco
    • Härtel, H., Kruse, E. and Grimm, B. (1997) Restriction of chlorophyll synthesis due to expression of glutamate 1-semialdehyde aminotransferase antisense RNA does not reduce the light-harvesting antenna size in tobacco. Plant Physiol. 113, 1113-1124.
    • (1997) Plant Physiol. , vol.113 , pp. 1113-1124
    • Härtel, H.1    Kruse, E.2    Grimm, B.3
  • 14
    • 0028069203 scopus 로고
    • Leaf developmental age controls expression of genes encoding enzymes of chlorophyll and heme biosynthesis in pea (Pisum sativum L.)
    • He, Z-H., Li, J., Sundqvist, C. and Timko, M.P. (1994) Leaf developmental age controls expression of genes encoding enzymes of chlorophyll and heme biosynthesis in pea (Pisum sativum L.). Plant Physiol. 106, 537-546.
    • (1994) Plant Physiol. , vol.106 , pp. 537-546
    • He, Z.-H.1    Li, J.2    Sundqvist, C.3    Timko, M.P.4
  • 15
    • 0001012359 scopus 로고
    • Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato {Solanum tuberosum
    • Höfgen, R. and Willmitzer, L. (1990) Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato {Solanum tuberosum). Plant Sci. 66, 221-230.
    • (1990) Plant Sci. , vol.66 , pp. 221-230
    • Höfgen, R.1    Willmitzer, L.2
  • 16
    • 0028208307 scopus 로고
    • A visible marker for antisense mRNA expression in plants: Inhibition of chlorophyll synthesis with a glutamate 1-semialdehyde aminotransferase antisense gene
    • Höfgen, R., Axelsen, K.B., Kannangara, C.G., Schüttke, I., Pohlenz, H.-D., Willmitzer, L., Grimm, B. and von Wettstein, D. (1994) A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate 1-semialdehyde aminotransferase antisense gene. Proc. Natl Acad. Sci. USA, 91, 1726-1730.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1726-1730
    • Höfgen, R.1    Axelsen, K.B.2    Kannangara, C.G.3    Schüttke, I.4    Pohlenz, H.-D.5    Willmitzer, L.6    Grimm, B.7    Von Wettstein, D.8
  • 18
    • 0022870544 scopus 로고
    • Genetic control of chlorophyll biosynthesis: Regulation of delta-aminolevulinate synthesis in Chlamydomonas
    • Huang, D.D. and Wang, W.-Y. (1986) Genetic control of chlorophyll biosynthesis: regulation of delta-aminolevulinate synthesis in Chlamydomonas. Mol. Gen. Genet. 205, 217-220
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 217-220
    • Huang, D.D.1    Wang, W.-Y.2
  • 19
    • 0002132016 scopus 로고
    • Biosynthesis of 5-aminolevulinic acid and its transformation into coproporpyhrinogen in animals and bacteria
    • Dailey, H.A., ed. New York: McGraw Hill
    • Jordan, P. (1990) Biosynthesis of 5-aminolevulinic acid and its transformation into coproporpyhrinogen in animals and bacteria. In Biosynthesis of Heme and Chlorophylls (Dailey, H.A., ed.). New York: McGraw Hill, pp. 55-121.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 55-121
    • Jordan, P.1
  • 21
    • 0022641077 scopus 로고
    • The nine amino-terminal residues of δ-aminolevulinate synthase direct β-galactosidase into the mitochondrial matrix
    • Keng, T., Alani, E. and Guarente, L. (1986) The nine amino-terminal residues of δ-aminolevulinate synthase direct β-galactosidase into the mitochondrial matrix. Mol. Cell. Biol. 6, 355-364.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 355-364
    • Keng, T.1    Alani, E.2    Guarente, L.3
  • 22
    • 0001336902 scopus 로고
    • The enzymic synthesis of 5-aminolevulinic acid
    • Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D. (1958) The enzymic synthesis of 5-aminolevulinic acid. J. Biol .Chem. 233, 1214-1219.
    • (1958) J. Biol .Chem. , vol.233 , pp. 1214-1219
    • Kikuchi, G.1    Kumar, A.2    Talmage, P.3    Shemin, D.4
  • 23
    • 0029151252 scopus 로고
    • Reduction of coproporphyrinogen oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidative defense system
    • Kruse, E., Mock, H.-P. and Grimm, B. (1995) Reduction of coproporphyrinogen oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidative defense system. EMBO J. 14, 3712-3720.
    • (1995) EMBO J. , vol.14 , pp. 3712-3720
    • Kruse, E.1    Mock, H.-P.2    Grimm, B.3
  • 24
    • 0004691482 scopus 로고
    • Targeting of protein to chloroplasts in transgenic tobacco by fusion to mutated transit peptide
    • Kuntz, M., Simons, A., Schell, J. and Schreier, P. (1986) Targeting of protein to chloroplasts in transgenic tobacco by fusion to mutated transit peptide. Mol. Gen. Genet. 205, 454-460.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 454-460
    • Kuntz, M.1    Simons, A.2    Schell, J.3    Schreier, P.4
  • 25
    • 0002634758 scopus 로고
    • Tetrapyrrole and heme biosynthesis in the yeast Saccharomyces cerevisiae
    • Dailey, H.A., ed. New York: McGraw Hill
    • Labbe-Bois, R. and Labbe, P. (1990) Tetrapyrrole and heme biosynthesis in the yeast Saccharomyces cerevisiae In Biosynthesis of Heme and Chlorophylls (Dailey, H.A., ed.). New York: McGraw Hill, pp. 235-285.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 235-285
    • Labbe-Bois, R.1    Labbe, P.2
  • 26
    • 77957068711 scopus 로고
    • Chlorophylls and carotinoids: Pigments of photosynthetic biomembranes
    • Lichtenthaler, H.K. (1987) Chlorophylls and carotinoids: pigments of photosynthetic biomembranes. Methods Enzymol. 148, 350-382.
    • (1987) Methods Enzymol. , vol.148 , pp. 350-382
    • Lichtenthaler, H.K.1
  • 28
    • 0028090388 scopus 로고
    • Glu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis
    • Glu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225, 529-537.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 529-537
    • Pontoppidan, B.1    Kannangara, C.G.2
  • 29
    • 0029926078 scopus 로고    scopus 로고
    • The regulation of enzymes involved in chlorophyll biosynthesis
    • Reinbothe, S. and Reinbothe, C. (1996) The regulation of enzymes involved in chlorophyll biosynthesis. Eur. J. Biochem. 237, 323-343.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 323-343
    • Reinbothe, S.1    Reinbothe, C.2
  • 31
    • 0027213464 scopus 로고
    • Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants
    • Smith, A.G., Marsh, O. and Elder, G.H. (1993), Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem. J. 249, 503-508.
    • (1993) Biochem. J. , vol.249 , pp. 503-508
    • Smith, A.G.1    Marsh, O.2    Elder, G.H.3
  • 32
    • 0000318222 scopus 로고
    • 5-aminolevulinic acid induced photodynamic damage of the photosynthetic electron transport chain of cucumber (Cucumis sativus L.) cotyledons
    • Tripathy, B.C. and Chakraborty, N. (1991) 5-aminolevulinic acid induced photodynamic damage of the photosynthetic electron transport chain of cucumber (Cucumis sativus L.) cotyledons. Plant Physiol. 96, 761-767.
    • (1991) Plant Physiol. , vol.96 , pp. 761-767
    • Tripathy, B.C.1    Chakraborty, N.2
  • 33
    • 31744433849 scopus 로고
    • Biosynthesis of α-aminoketones and the metabolism of aminoacetone
    • Urata, G. and Granick, S. (1963) Biosynthesis of α-aminoketones and the metabolism of aminoacetone. Biol. Chem. 238, 811-820.
    • (1963) Biol. Chem. , vol.238 , pp. 811-820
    • Urata, G.1    Granick, S.2
  • 34
    • 0023040119 scopus 로고
    • The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae
    • Urban-Grimal, D., Volland, C., Garnier, T., Dehoux, P. and Labbe-Bois, R. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur. J. Biochem. 156, 511-519.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 511-519
    • Urban-Grimal, D.1    Volland, C.2    Garnier, T.3    Dehoux, P.4    Labbe-Bois, R.5
  • 35
    • 0023898730 scopus 로고
    • The presequence of yeast 5-aminolevulinate synthase is not required for targeting to mitochondria
    • Volland, C. and Urban-Grimal, D. (1988) The presequence of yeast 5-aminolevulinate synthase is not required for targeting to mitochondria. J. Biol .Chem. 263, 8294-8299.
    • (1988) J. Biol .Chem. , vol.263 , pp. 8294-8299
    • Volland, C.1    Urban-Grimal, D.2
  • 36
    • 0021099519 scopus 로고
    • Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis
    • Weinstein, J.D. and Beale, S.I. (1983) Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis. J. Biol. Chem. 258, 6799-6807.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6799-6807
    • Weinstein, J.D.1    Beale, S.I.2
  • 37
    • 0010549081 scopus 로고
    • Isolation and characterization of a gene encoding meso-diaminopimelate dehydrogenase
    • Wenko, L.K., Treick, R.W. and Wilson, K.G. (1985) Isolation and characterization of a gene encoding meso-diaminopimelate dehydrogenase. Plant Mol. Biol. 4, 197-204.
    • (1985) Plant Mol. Biol. , vol.4 , pp. 197-204
    • Wenko, L.K.1    Treick, R.W.2    Wilson, K.G.3
  • 39
    • 0028972796 scopus 로고
    • Divergent pathways for δ-aminolevulinic acid synthesis in two species of Arthrobacter
    • Yang, H.-S. and Hoober, J.K. (1995). Divergent pathways for δ-aminolevulinic acid synthesis in two species of Arthrobacter. FEMS Microbiol. Lett. 134, 259-263.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 259-263
    • Yang, H.-S.1    Hoober, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.