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Volumn 208, Issue 2, 1999, Pages 264-273

Expression studies in tetrapyrrole biosynthesis: Inverse maxima of magnesium chelatase and ferrochelatase activity during cyclic photoperiods

Author keywords

Chlorophyll; Chloroplast; Circadian rhythm; Heme; Nicotiana (tetrapyrroles); Pigment synthesis

Indexed keywords

AMINOLEVULINIC ACID; BIOSYNTHESIS; CHLOROPHYLL; ENZYME ACTIVITY; FERROCHELATASE; MAGNESIUM CHELATASE; PLANT METABOLISM;

EID: 0032901677     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050558     Document Type: Article
Times cited : (126)

References (47)
  • 1
    • 0002383191 scopus 로고
    • Tetrapyrrole metabolism in photosynthetic organisms
    • Dailey HA (ed) McGraw-Hill, New York
    • Beale SI, Weinstein JD (1990) Tetrapyrrole metabolism in photosynthetic organisms. In: Dailey HA (ed) Biosynthesis of heme and chlorophylls. McGraw-Hill, New York, pp 287-391
    • (1990) Biosynthesis of Heme and Chlorophylls
    • Beale, S.I.1    Weinstein, J.D.2
  • 2
    • 0001575727 scopus 로고
    • The circadian oscillator coordinates the synthesis of apoproteins and their pigments during chloroplast development
    • Beator J, Kloppstech K (1993) The circadian oscillator coordinates the synthesis of apoproteins and their pigments during chloroplast development. Plant Physiol 103: 191-196
    • (1993) Plant Physiol , vol.103 , pp. 191-196
    • Beator, J.1    Kloppstech, K.2
  • 3
    • 0000071851 scopus 로고
    • Circadian rhythmicity in the expression of genes in higher plants
    • Beator J, Kloppstech K (1994) Circadian rhythmicity in the expression of genes in higher plants. Mol Biol (Life Sci Adv) 13: 203-219
    • (1994) Mol Biol (Life Sci Adv) , vol.13 , pp. 203-219
    • Beator, J.1    Kloppstech, K.2
  • 4
    • 11944265619 scopus 로고
    • The effect of heat shock on morphogenesis in barley
    • Beator J, Pötter E, Kloppstech K (1992) The effect of heat shock on morphogenesis in barley. Plant Physiol 100: 1780-1786
    • (1992) Plant Physiol , vol.100 , pp. 1780-1786
    • Beator, J.1    Pötter, E.2    Kloppstech, K.3
  • 5
    • 0011390341 scopus 로고
    • Circadian expression of the light-harvesting protein of photosystem II in etiolated bean leaves following a single red light pulse: Coordination with the capacity of the plant to form chlorophyll and the thylakoid-bound protease
    • Bei-Paraskevopoulou T, Anastassiou R, Agryroudi-Akoyuonoglou J (1995) Circadian expression of the light-harvesting protein of photosystem II in etiolated bean leaves following a single red light pulse: coordination with the capacity of the plant to form chlorophyll and the thylakoid-bound protease. Photosynth Res 44: 93-106
    • (1995) Photosynth Res , vol.44 , pp. 93-106
    • Bei-Paraskevopoulou, T.1    Anastassiou, R.2    Agryroudi-Akoyuonoglou, J.3
  • 6
    • 0030162258 scopus 로고    scopus 로고
    • Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley
    • Bougri O, Grimm B (1996) Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley. Plant J 9: 867-878
    • (1996) Plant J , vol.9 , pp. 867-878
    • Bougri, O.1    Grimm, B.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification 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
  • 8
    • 0001114634 scopus 로고
    • Die endogene tagesrhythmik als grundlage der photoperiodischen reaktion
    • Bünning E (1936) Die endogene Tagesrhythmik als Grundlage der photoperiodischen Reaktion. Ber Dtsch Bot Ges 54: 590-607
    • (1936) Ber Dtsch Bot Ges , vol.54 , pp. 590-607
    • Bünning, E.1
  • 9
    • 0024297135 scopus 로고
    • Purification and properties of ferrochelatase from the yeast Saccharomyces cerevisiae
    • Camadro JM, Labbe P (1988) Purification and properties of ferrochelatase from the yeast Saccharomyces cerevisiae. J Biol Chem 263: 11675-11682
    • (1988) J Biol Chem , vol.263 , pp. 11675-11682
    • Camadro, J.M.1    Labbe, P.2
  • 10
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczinsky P, 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
  • 11
    • 0028146669 scopus 로고
    • The bacteriochlorophyll biosynthesis gene, bchM, of Rhodobacter sphaeroides encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase
    • Gibson LCD, Hunter CN (1994) The bacteriochlorophyll biosynthesis gene, bchM, of Rhodobacter sphaeroides encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase. FEBS Lett 352: 127-130
    • (1994) FEBS Lett , vol.352 , pp. 127-130
    • Gibson, L.C.D.1    Hunter, C.N.2
  • 13
    • 0028951161 scopus 로고
    • Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: Reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli
    • Gibson LCD, Willows RD, Kannangara CG, von Wettstein D, Hunter CN (1995) Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli. Proc Natl Acad Sci USA 92: 1941-1944
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1941-1944
    • Gibson, L.C.D.1    Willows, R.D.2    Kannangara, C.G.3    Von Wettstein, D.4    Hunter, C.N.5
  • 14
    • 0024234261 scopus 로고
    • A light-entrained circadian clock controls transcription of several plant genes
    • Giuliano G, Hoffmann NE, Ko K, Scolnik PA, Cashmore AR (1988) A light-entrained circadian clock controls transcription of several plant genes. EMBO J 7: 3635-3642
    • (1988) EMBO J , vol.7 , pp. 3635-3642
    • Giuliano, G.1    Hoffmann, N.E.2    Ko, K.3    Scolnik, P.A.4    Cashmore, A.R.5
  • 15
    • 0032082554 scopus 로고    scopus 로고
    • Novel insights in the control of tetrapyrrole metabolism of higher plants
    • Grimm B (1998) Novel insights in the control of tetrapyrrole metabolism of higher plants. Curr Opin Plant Biol 1: 245-250
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 245-250
    • Grimm, B.1
  • 16
    • 0030695453 scopus 로고    scopus 로고
    • ATPase and phosphate exchange activities in magnesium chelatase subunits of Rhodobacter sphaeroides
    • Hansson M, Kannangara CG (1997) ATPase and phosphate exchange activities in magnesium chelatase subunits of Rhodobacter sphaeroides. Proc Natl Acad Sci USA 94: 13351-13356
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13351-13356
    • Hansson, M.1    Kannangara, C.G.2
  • 17
    • 0027296056 scopus 로고
    • Olive: A key gene required for chlorophyll biosynthesis in Antirrhinum majus
    • Hudson A, Carpenter R, Doyle R, Coen ES (1993) Olive: a key gene required for chlorophyll biosynthesis in Antirrhinum majus. EMBO J 12: 3711-3719
    • (1993) EMBO J , vol.12 , pp. 3711-3719
    • Hudson, A.1    Carpenter, R.2    Doyle, R.3    Coen, E.S.4
  • 19
    • 0001589893 scopus 로고
    • Biosynthesis of Δ-aminolevulinate in greening barley leaves II: Induction of enzyme synthesis by light
    • Kannangara CG, Gough SP (1979) Biosynthesis of Δ-aminolevulinate in greening barley leaves II: induction of enzyme synthesis by light. Carlsberg Res Commun 44: 11-20
    • (1979) Carlsberg Res Commun , vol.44 , pp. 11-20
    • Kannangara, C.G.1    Gough, S.P.2
  • 20
    • 0000776173 scopus 로고
    • Diurnal and circadian rhythmicity in the expression of light-induced plant nuclear messenger RNAs
    • Kloppstech K (1985) Diurnal and circadian rhythmicity in the expression of light-induced plant nuclear messenger RNAs. Planta 165: 502-506
    • (1985) Planta , vol.165 , pp. 502-506
    • Kloppstech, K.1
  • 21
    • 0025228868 scopus 로고
    • Isolation of a gene encoding a novel chloroplast protein by T-DNA tagging in Arabidopsis thaliana
    • Koncz C, Meyerhofer R, Koncz-Kalman Z, Nawrath C, Reiss B, Redei GP, Schell J (1990) Isolation of a gene encoding a novel chloroplast protein by T-DNA tagging in Arabidopsis thaliana. EMBO J 9: 1337-1346
    • (1990) EMBO J , vol.9 , pp. 1337-1346
    • Koncz, C.1    Meyerhofer, R.2    Koncz-Kalman, Z.3    Nawrath, C.4    Reiss, B.5    Redei, G.P.6    Schell, J.7
  • 22
    • 0031439546 scopus 로고    scopus 로고
    • Chlorophyll precursors are signals of chloroplast origin involved in light induction of nuclear heat-shock genes
    • Kropat J, Oster U, Rüdiger W, Beck CF (1997) Chlorophyll precursors are signals of chloroplast origin involved in light induction of nuclear heat-shock genes. Proc Natl Acad Sci USA 94: 14168-14172
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14168-14172
    • Kropat, J.1    Oster, U.2    Rüdiger, W.3    Beck, C.F.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 HP, 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
    • 0030988808 scopus 로고    scopus 로고
    • Developmental and circadian control of the capacity for δ-aminolevulinic acid synthesis in green barley
    • Kruse E, Grimm B, Beator J, Kloppstech K (1997) Developmental and circadian control of the capacity for δ-aminolevulinic acid synthesis in green barley. Planta 202: 235-241
    • (1997) Planta , vol.202 , pp. 235-241
    • Kruse, E.1    Grimm, B.2    Beator, J.3    Kloppstech, K.4
  • 25
    • 0000498405 scopus 로고
    • Chloroplast biogenesis 65: Enzymic conversion of protoporphyrin IX to Mg-protoporphyrin IX in a subplastidic membrane fraction of cucumber etiochloroplasts
    • Lee HJ, Ball MD, Parham R, Rebeiz CA (1992) Chloroplast biogenesis 65: enzymic conversion of protoporphyrin IX to Mg-protoporphyrin IX in a subplastidic membrane fraction of cucumber etiochloroplasts. Plant Physiol 99: 1134-1140
    • (1992) Plant Physiol , vol.99 , pp. 1134-1140
    • Lee, H.J.1    Ball, M.D.2    Parham, R.3    Rebeiz, C.A.4
  • 26
    • 0023614235 scopus 로고
    • An HPLC assay for rat liver ferrochelatase activity
    • Li F, Lim CK, Peters TJ (1987) An HPLC assay for rat liver ferrochelatase activity. Biochem Chromatogr 2: 164-168
    • (1987) Biochem Chromatogr , vol.2 , pp. 164-168
    • Li, F.1    Lim, C.K.2    Peters, T.J.3
  • 27
    • 0026722463 scopus 로고
    • Localization within the chloroplasts of protoporphyrinogen oxidase the target enzyme for diphenylether-like herbicides
    • Matringe M, Camadro JM, Block MA, Joyard J, Scalla R, Labbe P, Douce R (1992) Localization within the chloroplasts of protoporphyrinogen oxidase the target enzyme for diphenylether-like herbicides. J Biol Chem 267: 4646-4651
    • (1992) J Biol Chem , vol.267 , pp. 4646-4651
    • Matringe, M.1    Camadro, J.M.2    Block, M.A.3    Joyard, J.4    Scalla, R.5    Labbe, P.6    Douce, R.7
  • 28
    • 0028342982 scopus 로고
    • Localization of ferrochelatase activity within mature pea chloroplasts
    • Matringe M, Camadro JM, Joyard J, Douce R (1994) Localization of ferrochelatase activity within mature pea chloroplasts. J Biol Chem 269: 15010-15015
    • (1994) J Biol Chem , vol.269 , pp. 15010-15015
    • Matringe, M.1    Camadro, J.M.2    Joyard, J.3    Douce, R.4
  • 29
    • 0031007125 scopus 로고    scopus 로고
    • Reduction of uroporphyrinogen decarboxylase by antisense RNA expression affects activities of other enzymes involved in tetrapyrrole biosynthesis and leads to light-dependent necrosis
    • Mock HP, Grimm B (1997) Reduction of uroporphyrinogen decarboxylase by antisense RNA expression affects activities of other enzymes involved in tetrapyrrole biosynthesis and leads to light-dependent necrosis. Plant Physiol 113: 1101-1112
    • (1997) Plant Physiol , vol.113 , pp. 1101-1112
    • Mock, H.P.1    Grimm, B.2
  • 30
    • 0001622785 scopus 로고
    • A circadian clock regulates transcription of the wheat Cab-1 gene
    • Nagy F, Kay SA, Chua NH (1988) A circadian clock regulates transcription of the wheat Cab-1 gene. Genes Dev 2: 376-382
    • (1988) Genes Dev , vol.2 , pp. 376-382
    • Nagy, F.1    Kay, S.A.2    Chua, N.H.3
  • 31
    • 0028928946 scopus 로고
    • The steady state mRNA levels for thylakoid proteins exhibit coordinate diurnal regulation
    • Oelmüller R, Schneiderbauer A, Herrmann RG, Kloppstech K (1995) The steady state mRNA levels for thylakoid proteins exhibit coordinate diurnal regulation. Mol Gen Genet 246: 478-484
    • (1995) Mol Gen Genet , vol.246 , pp. 478-484
    • Oelmüller, R.1    Schneiderbauer, A.2    Herrmann, R.G.3    Kloppstech, K.4
  • 32
    • 0031279340 scopus 로고    scopus 로고
    • Mg-chelatase of tobacco: Identification of a Chl D cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the yeast two-hybrid system and reconstitution of the enzyme activity by co-expression of recombinant CHL D, CHL H and CHL I
    • Papenbrock J, Gräfe S, Kruse E, Hänel F, Grimm B (1997) Mg-chelatase of tobacco: Identification of a Chl D cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the yeast two-hybrid system and reconstitution of the enzyme activity by co-expression of recombinant CHL D, CHL H and CHL I. Plant J 12: 981-990
    • (1997) Plant J , vol.12 , pp. 981-990
    • Papenbrock, J.1    Gräfe, S.2    Kruse, E.3    Hänel, F.4    Grimm, B.5
  • 33
    • 0028872256 scopus 로고
    • Light-harvesting chlorophyll a/b complexes: Interdependent pigment synthesis and protein assembly
    • Plumley FG, Schmidt GW (1995). Light-harvesting chlorophyll a/b complexes: interdependent pigment synthesis and protein assembly. Plant Cell 7: 689-704
    • (1995) Plant Cell , vol.7 , pp. 689-704
    • Plumley, F.G.1    Schmidt, G.W.2
  • 34
    • 0031688469 scopus 로고    scopus 로고
    • Light-dependent increase in chlorophyll precursors during the day-night cycle in tobacco and barley seedlings
    • Pöpperl G, Oster U, Rüdiger W (1998). Light-dependent increase in chlorophyll precursors during the day-night cycle in tobacco and barley seedlings. J Plant Physiol 153: 40-45
    • (1998) J Plant Physiol , vol.153 , pp. 40-45
    • Pöpperl, G.1    Oster, U.2    Rüdiger, W.3
  • 35
    • 26044440113 scopus 로고
    • Determination of accurate coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectrocopy
    • Porra RJ, Thompson WA, Kriedemann PE (1989) Determination of accurate coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectrocopy. Biochim Biophys Acta 975: 384-394
    • (1989) Biochim Biophys Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 36
    • 0031007284 scopus 로고    scopus 로고
    • The molecular localisation of ferrochelatase in higher plants
    • Roper JM, Smith AG (1997) The molecular localisation of ferrochelatase in higher plants. Eur J Biochem 246: 32-37
    • (1997) Eur J Biochem , vol.246 , pp. 32-37
    • Roper, J.M.1    Smith, A.G.2
  • 38
    • 0000441055 scopus 로고
    • Biosynthesis of protoheme and heme a from glutamate in maize
    • Schneegurt MA, Beale SI (1986) Biosynthesis of protoheme and heme a from glutamate in maize. Plant Physiol 81: 965-971
    • (1986) Plant Physiol , vol.81 , pp. 965-971
    • Schneegurt, M.A.1    Beale, S.I.2
  • 39
    • 0024286451 scopus 로고
    • Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoopint) species
    • Smith AG (1988) Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoopint) species. Biochem J 249: 423-428
    • (1988) Biochem J , vol.249 , pp. 423-428
    • Smith, A.G.1
  • 40
    • 0003296584 scopus 로고
    • Enzymes of chlorophyll and heme biosynthesis
    • Dey PM, Harborne JB (eds) Academic Press, London
    • Smith AG, Griffiths WT (1993) Enzymes of chlorophyll and heme biosynthesis. In: Dey PM, Harborne JB (eds) Methods in plant biochemistry, vol 9. Academic Press, London, pp 299-343
    • (1993) Methods in Plant Biochemistry , vol.9 , pp. 299-343
    • Smith, A.G.1    Griffiths, W.T.2
  • 41
    • 0028305713 scopus 로고
    • Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant
    • Smith AG, Santana MA, Wallace-Cook ADM, Roper JM, Labbe-Bois R (1994) Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant. J Biol Chem 269: 13405-13413
    • (1994) J Biol Chem , vol.269 , pp. 13405-13413
    • Smith, A.G.1    Santana, M.A.2    Wallace-Cook, A.D.M.3    Roper, J.M.4    Labbe-Bois, R.5
  • 42
    • 0011435340 scopus 로고
    • Circadian rhythm in the expression of the mRNA coding for the apoprotein of the light harvesting complex of photosystem II. Phytochrome control and persistent far-red reversibility
    • Tavladoraki P, Kloppstech K, Argyroudi-Akoyunoglou JH (1989) Circadian rhythm in the expression of the mRNA coding for the apoprotein of the light harvesting complex of photosystem II. Phytochrome control and persistent far-red reversibility. Plant Physiol 90: 665-672
    • (1989) Plant Physiol , vol.90 , pp. 665-672
    • Tavladoraki, P.1    Kloppstech, K.2    Argyroudi-Akoyunoglou, J.H.3
  • 43
    • 0024605991 scopus 로고
    • Transcriptional regulation by a circadian rhythm
    • Taylor WC (1989) Transcriptional regulation by a circadian rhythm. Plant Cell 1: 259-264
    • (1989) Plant Cell , vol.1 , pp. 259-264
    • Taylor, W.C.1
  • 45
    • 0030899819 scopus 로고    scopus 로고
    • Comparative study of heme and Mg-protoporphyrin (monomethyl ester) biosyntheis in isolated pea chloroplasts: Effects of ATP and metal ions
    • Walker CJ, Yu GH, Weinstein JD (1997) Comparative study of heme and Mg-protoporphyrin (monomethyl ester) biosyntheis in isolated pea chloroplasts: effects of ATP and metal ions. Plant Physiol Biochem 35: 213-221
    • (1997) Plant Physiol Biochem , vol.35 , pp. 213-221
    • Walker, C.J.1    Yu, G.H.2    Weinstein, J.D.3
  • 46
    • 0021099519 scopus 로고
    • Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis
    • Weinstein JD, Beale SI (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


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