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Volumn 109, Issue 3, 2000, Pages 298-303

Protochlorophyllide-independent import of two NADPH:Pchlide oxidoreductase proteins (PORA and PORB) from barley into isolated plastids

Author keywords

[No Author keywords available]

Indexed keywords

AMINOLEVULINIC ACID; BARLEY; CATALYSIS; CHLOROPHYLLIDE; CHLOROPLAST; ENZYME PRECURSOR; GREENHOUSE; PEA; PLASTID; PROTEIN DEGRADATION; PROTEIN TRANSPORT; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE; REDUCTION;

EID: 0033945607     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.2000.100311.x     Document Type: Article
Times cited : (38)

References (28)
  • 1
    • 0029346958 scopus 로고
    • Identification of NADPH:Pchlide oxidoreductases A and B: A branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana
    • Armstrong GA, Runge S, Frick G, Sperling U, Apel K (1995) Identification of NADPH:Pchlide oxidoreductases A and B: A branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol 108: 1505-1517
    • (1995) Plant Physiol , vol.108 , pp. 1505-1517
    • Armstrong, G.A.1    Runge, S.2    Frick, G.3    Sperling, U.4    Apel, K.5
  • 2
    • 0342848648 scopus 로고    scopus 로고
    • Characterisation of the plastid import reaction of the pea NADPH:Pchlide oxidoreductase (POR)
    • Argyroudi-Akoyunoglou JH, Senger H (eds) Crete, Greece, August 10-15 1998. Kluwer Academic Publishers, Dordrecht
    • Aronsson H, Almkvist J, Sundqvist C, Timko MP, Dahlin C (1999) Characterisation of the plastid import reaction of the pea NADPH:Pchlide oxidoreductase (POR). In: Argyroudi-Akoyunoglou JH, Senger H (eds) The Chloroplast: From Molecular Biology to Biotechnology. Crete, Greece, August 10-15 1998. Kluwer Academic Publishers, Dordrecht, pp 167-170
    • (1999) The Chloroplast: From Molecular Biology to Biotechnology , pp. 167-170
    • Aronsson, H.1    Almkvist, J.2    Sundqvist, C.3    Timko, M.P.4    Dahlin, C.5
  • 3
    • 84989762252 scopus 로고
    • Import of nuclear-encoded proteins into carotenoid-deficient young etioplasts
    • Dahlin C (1993) Import of nuclear-encoded proteins into carotenoid-deficient young etioplasts. Physiol Plant 87: 410-416
    • (1993) Physiol Plant , vol.87 , pp. 410-416
    • Dahlin, C.1
  • 4
    • 0028003222 scopus 로고
    • Integration of nuclear-encoded proteins into pea thylakoids with different pigment contents
    • Dahlin C, Timko MP (1994) Integration of nuclear-encoded proteins into pea thylakoids with different pigment contents. Physiol Plant 91: 212-218
    • (1994) Physiol Plant , vol.91 , pp. 212-218
    • Dahlin, C.1    Timko, M.P.2
  • 5
    • 0000126254 scopus 로고
    • Formation of mg-containing chlorophyll precursors from protoporphyrin IX, δ-aminolevulinic acid and glutamate in isolated, photosynthetically competent, developing chloroplasts
    • Fuesler TP, Castelfranco PA, Wong Y (1984) Formation of Mg-containing chlorophyll precursors from protoporphyrin IX, δ-aminolevulinic acid and glutamate in isolated, photosynthetically competent, developing chloroplasts. Plant Physiol 74: 928-933
    • (1984) Plant Physiol , vol.74 , pp. 928-933
    • Fuesler, T.P.1    Castelfranco, P.A.2    Wong, Y.3
  • 6
    • 51249179257 scopus 로고
    • The presence and photoregulation of protochlorophyllide reductase in green tissues
    • Griffiths WT, Kay SA, Oliver RP (1985) The presence and photoregulation of protochlorophyllide reductase in green tissues. Plant Mol Biol 4: 13-22
    • (1985) Plant Mol Biol , vol.4 , pp. 13-22
    • Griffiths, W.T.1    Kay, S.A.2    Oliver, R.P.3
  • 7
    • 0028961554 scopus 로고
    • Two routes of Chlide synthesis that are differentially regulated by light in barley (Hordeum vulgare L.)
    • Holtorf H, Reinbothe S, Reinbothe C, Bereza B, Ape K (1995) Two routes of Chlide synthesis that are differentially regulated by light in barley (Hordeum vulgare L.). Proc Natl Acad Sci USA 92: 3254-3258
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3254-3258
    • Holtorf, H.1    Reinbothe, S.2    Reinbothe, C.3    Bereza, B.4    Ape, K.5
  • 8
    • 0000668045 scopus 로고
    • Light-induced breakdown of NADPH-pchlide oxidoreductase in vitro
    • Kay S, Griffiths T (1983) Light-induced breakdown of NADPH-pchlide oxidoreductase in vitro. Plant Physiol 72: 229-236
    • (1983) Plant Physiol , vol.72 , pp. 229-236
    • Kay, S.1    Griffiths, T.2
  • 9
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra K, Cline K (1999) Protein import and routing systems of chloroplasts. Plant Cell 11: 557-570
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 10
    • 0002352058 scopus 로고
    • Effect of light, developmental age and phytohormones on the expression of the gene encoding NADPH-Pchlide oxidoreductase in Cucumis sativus
    • Kuroda H, Masuda T, Ohta H, Shioi Y, Takamiya K (1396) Effect of light, developmental age and phytohormones on the expression of the gene encoding NADPH-Pchlide oxidoreductase in Cucumis sativus. Plant Physiol Biochem 34: 17-22
    • (1396) Plant Physiol Biochem , vol.34 , pp. 17-22
    • Kuroda, H.1    Masuda, T.2    Ohta, H.3    Shioi, Y.4    Takamiya, K.5
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 12
    • 0000252516 scopus 로고
    • Detection of protochlorophyllide forms in irradiated green leaves and chloroplasts by difference fluorescence spectroscopy at 77 K
    • Lebedev NN, Siffel P, Kransovskii AA (1985) Detection of protochlorophyllide forms in irradiated green leaves and chloroplasts by difference fluorescence spectroscopy at 77 K. Photosynthetica 19: 183-187
    • (1985) Photosynthetica , vol.19 , pp. 183-187
    • Lebedev, N.N.1    Siffel, P.2    Kransovskii, A.A.3
  • 13
    • 0000444532 scopus 로고
    • Determination of total carotenoids and chlorophylls a and h of leaf extracts in different solvents
    • Lichtenthaler HK, Wellburn AR (1983) Determination of total carotenoids and chlorophylls a and h of leaf extracts in different solvents. Biochem Soc Trans 603: 591-592
    • (1983) Biochem Soc Trans , vol.603 , pp. 591-592
    • Lichtenthaler, H.K.1    Wellburn, A.R.2
  • 14
    • 85011847403 scopus 로고
    • The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Triticum aestivum) as revealed by silver staining
    • Lindsten A, Ryberg M, Sundqvist C (1988) The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Triticum aestivum) as revealed by silver staining. Physiol Plant 72: 167-176
    • (1988) Physiol Plant , vol.72 , pp. 167-176
    • Lindsten, A.1    Ryberg, M.2    Sundqvist, C.3
  • 15
    • 0019041296 scopus 로고
    • Light modulation of the activity of protochlorophyllide reductase
    • Mapleston RE, Griffiths WT (1980) Light modulation of the activity of protochlorophyllide reductase. Biochem J 189: 125-134
    • (1980) Biochem J , vol.189 , pp. 125-134
    • Mapleston, R.E.1    Griffiths, W.T.2
  • 16
    • 0033030860 scopus 로고    scopus 로고
    • Chloroplast precursor protein translocon
    • May T, Soll J (1999) Chloroplast precursor protein translocon. FEBS Lett 452: 52-56
    • (1999) FEBS Lett , vol.452 , pp. 52-56
    • May, T.1    Soll, J.2
  • 17
    • 0029201048 scopus 로고
    • Two NADPH:Pchlide oxidoreductases in barley: Evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings
    • Reinbothe S, Reinbothe C, Holtorf H, Apel K (1995a) Two NADPH:Pchlide oxidoreductases in barley: Evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings. Plant Cell 7: 1933-1940
    • (1995) Plant Cell , vol.7 , pp. 1933-1940
    • Reinbothe, S.1    Reinbothe, C.2    Holtorf, H.3    Apel, K.4
  • 18
    • 0029240288 scopus 로고
    • Substrat-dependent transport of the NADPH:Pchlide oxidoreductase into isolated plastids
    • Reinbothe S, Runge S, Reinbothe C, van Cleve B, Apel K (1995b) Substrat-dependent transport of the NADPH:Pchlide oxidoreductase into isolated plastids. Plant Cell 7: 161-172
    • (1995) Plant Cell , vol.7 , pp. 161-172
    • Reinbothe, S.1    Runge, S.2    Reinbothe, C.3    Van Cleve, B.4    Apel, K.5
  • 19
    • 0028784796 scopus 로고
    • A light-induced protease from barley plastids degrades NADPH:Pchlide oxidoreductase complexed with chlorophyllide
    • Reinbothe C, Apel K, Reinbothe S (1995c) A light-induced protease from barley plastids degrades NADPH:Pchlide oxidoreductase complexed with chlorophyllide. Mol Cell Biol 15: 6206-6212
    • (1995) Mol Cell Biol , vol.15 , pp. 6206-6212
    • Reinbothe, C.1    Apel, K.2    Reinbothe, S.3
  • 20
    • 0030872725 scopus 로고    scopus 로고
    • Regulation of chloroplast protein import through a protochlorophyllide-responsive transit peptide
    • Reinbothe C, Lebedev N, Apel K, Reinbothe S (1997) Regulation of chloroplast protein import through a protochlorophyllide-responsive transit peptide. Proc Natl Acad Sci USA 94: 8890-8894
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8890-8894
    • Reinbothe, C.1    Lebedev, N.2    Apel, K.3    Reinbothe, S.4
  • 21
    • 0030131174 scopus 로고    scopus 로고
    • Distinct roles for light-dependent NADPH:Protochlorophyllide oxidoreductases (POR) A and B during greening in higher plants
    • Runge S, Sperling U, Frick G, Apel K, Armstrong GA (1996) Distinct roles for light-dependent NADPH:protochlorophyllide oxidoreductases (POR) A and B during greening in higher plants. Plant J 9: 513-523
    • (1996) Plant J , vol.9 , pp. 513-523
    • Runge, S.1    Sperling, U.2    Frick, G.3    Apel, K.4    Armstrong, G.A.5
  • 22
    • 0019046758 scopus 로고
    • Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes
    • Rüdiger W, Bentz J, Guthoff C (1980) Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes. Eur J Biochem 109: 193-200
    • (1980) Eur J Biochem , vol.109 , pp. 193-200
    • Rüdiger, W.1    Bentz, J.2    Guthoff, C.3
  • 23
    • 0001084795 scopus 로고
    • Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies
    • Ryberg M, Dehesh K (1986) Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies. Physiol Plant 66: 616-624
    • (1986) Physiol Plant , vol.66 , pp. 616-624
    • Ryberg, M.1    Dehesh, K.2
  • 24
    • 0019638822 scopus 로고
    • The protochlorophyllide holochrome of barley (Hordeum vulgare L.). The effect of light on the NADPH-protochlorophyllide oxidoreductase
    • Santel HJ, Apel K (1981) The protochlorophyllide holochrome of barley (Hordeum vulgare L.). The effect of light on the NADPH-protochlorophyllide oxidoreductase. Eur J Biochem 120: 95-103
    • (1981) Eur J Biochem , vol.120 , pp. 95-103
    • Santel, H.J.1    Apel, K.2
  • 25
    • 0026824270 scopus 로고
    • Molecular cloning, nuclear gene structure, and developmental expression of NADPH:Protochlorophyllide oxidoreductase in pea (Pisum sativum L.)
    • Spano AJ, He Z, Michel H, Hunt DF, Timko MP (1992) Molecular cloning, nuclear gene structure, and developmental expression of NADPH:protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol Biol 18: 967-972
    • (1992) Plant Mol Biol , vol.18 , pp. 967-972
    • Spano, A.J.1    He, Z.2    Michel, H.3    Hunt, D.F.4    Timko, M.P.5
  • 26
    • 0032004065 scopus 로고    scopus 로고
    • Etioplast differentiation in Arabidopsis: Both PORA and PORB restore the prolamellar body and photoactive protochlorophyllide-F655 to the cop 1 photomorphogenic mutant
    • Sperling U, Franck F, van Cleve B, Frick G, Apel K, Armstrong GA (1998) Etioplast differentiation in Arabidopsis: Both PORA and PORB restore the prolamellar body and photoactive protochlorophyllide-F655 to the cop 1 photomorphogenic mutant. Plant Cell 10: 283-296
    • (1998) Plant Cell , vol.10 , pp. 283-296
    • Sperling, U.1    Franck, F.2    Van Cleve, B.3    Frick, G.4    Apel, K.5    Armstrong, G.A.6
  • 27
    • 84981566338 scopus 로고
    • The pool size of protochlorophyllide during different stages of greening of dark grown wheat leaves
    • Sundqvist C (1974) The pool size of protochlorophyllide during different stages of greening of dark grown wheat leaves. Physiol Plant 30: 143-147
    • (1974) Physiol Plant , vol.30 , pp. 143-147
    • Sundqvist, C.1
  • 28
    • 0030869207 scopus 로고    scopus 로고
    • With chlorophyll pigments from prolamellar bodies to light-harvesting complexes
    • Sundqvist C, Dahlin C (1997) With chlorophyll pigments from prolamellar bodies to light-harvesting complexes. Physiol Plant 100: 748-759
    • (1997) Physiol Plant , vol.100 , pp. 748-759
    • Sundqvist, C.1    Dahlin, C.2


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