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Volumn 1716, Issue 2, 2005, Pages 97-103

Organization of protochlorophyllide oxidoreductase in prolamellar bodies isolated from etiolated carotenoid-deficient wheat leaves as revealed by fluorescence probes

Author keywords

Carotenoid; Fluorescence probe; NADPH protochlorophyllide oxidoreductase; Norflurazon; Prolamellar body

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CAROTENOID; FATTY ACID; FLUORESCENT DYE; MEMBRANE LIPID; OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; PYRENE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 27444434316     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2005.09.001     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 0019076379 scopus 로고
    • Identification of the polypeptides of NADPH-protochlorophyllide oxidoreductase
    • R.P. Oliver, and W.T. Griffiths Identification of the polypeptides of NADPH-protochlorophyllide oxidoreductase Biochem. J. 191 1980 227 280
    • (1980) Biochem. J. , vol.191 , pp. 227-280
    • Oliver, R.P.1    Griffiths, W.T.2
  • 2
    • 0001633977 scopus 로고
    • Pigment-protein complexes in illuminated etiolated leaves
    • R.P. Oliver, and W.T. Griffiths Pigment-protein complexes in illuminated etiolated leaves Plant Physiol. 70 1982 1019 1025
    • (1982) Plant Physiol. , vol.70 , pp. 1019-1025
    • Oliver, R.P.1    Griffiths, W.T.2
  • 3
    • 0019073797 scopus 로고
    • The Pchlide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH:protochloriphyllide oxidoreductase
    • K. Apel, H.J. Santel, T.E. Redlinger, and H. Falk The Pchlide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH:protochloriphyllide oxidoreductase Eur. J. Biochem. 111 1980 251 258
    • (1980) Eur. J. Biochem. , vol.111 , pp. 251-258
    • Apel, K.1    Santel, H.J.2    Redlinger, T.E.3    Falk, H.4
  • 4
    • 84987044119 scopus 로고
    • Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts
    • M. Ryberg, and C. Sundqvist Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts Physiol. Plant. 56 1982 125 132
    • (1982) Physiol. Plant. , vol.56 , pp. 125-132
    • Ryberg, M.1    Sundqvist, C.2
  • 5
    • 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
    • M. Ryberg, and K. Dehesh 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 1986 616 624
    • (1986) Physiol. Plant. , vol.66 , pp. 616-624
    • Ryberg, M.1    Dehesh, K.2
  • 6
    • 0030869207 scopus 로고    scopus 로고
    • With chlorophyll pigments from prolamellar bodies to light-harvesting complexes
    • C. Sundqvist, and C. Dahlin With chlorophyll pigments from prolamellar bodies to light-harvesting complexes Physiol. Plant. 100 1997 748 759
    • (1997) Physiol. Plant. , vol.100 , pp. 748-759
    • Sundqvist, C.1    Dahlin, C.2
  • 7
    • 0000241452 scopus 로고
    • The formation of a short-wavelength chlorophyllide form at partial phototransformation of protochlorophyllide in etioplast inner membranes
    • B. Böddi, M. Ryberg, and C. Sundqvist The formation of a short-wavelength chlorophyllide form at partial phototransformation of protochlorophyllide in etioplast inner membranes Photochem. Photobiol. 53 1991 667 673
    • (1991) Photochem. Photobiol. , vol.53 , pp. 667-673
    • Böddi, B.1    Ryberg, M.2    Sundqvist, C.3
  • 8
    • 84989665833 scopus 로고
    • Isoelectric focusing of pigment-protein complexes solubilized from non-irradiated and irradiated prolamellar bodies
    • B. Wiktorsson, M. Ryberg, S. Gough, and C. Sundqvist Isoelectric focusing of pigment-protein complexes solubilized from non-irradiated and irradiated prolamellar bodies Physiol. Plant. 85 1992 659 669
    • (1992) Physiol. Plant. , vol.85 , pp. 659-669
    • Wiktorsson, B.1    Ryberg, M.2    Gough, S.3    Sundqvist, C.4
  • 9
    • 0001402677 scopus 로고
    • The effect of cross-linking of the subunits on NADPH-protochlorophyllide oxidoreductase on the aggregational state of protochlorophyllide
    • B. Wiktorsson, S. Engdahl, L.B. Zhong, B. Boddi, M. Ryberg, and C. Sundquvist The effect of cross-linking of the subunits on NADPH- protochlorophyllide oxidoreductase on the aggregational state of protochlorophyllide Photosynthesis 29 1993 205 218
    • (1993) Photosynthesis , vol.29 , pp. 205-218
    • Wiktorsson, B.1    Engdahl, S.2    Zhong, L.B.3    Boddi, B.4    Ryberg, M.5    Sundquvist, C.6
  • 10
    • 0032579331 scopus 로고    scopus 로고
    • X-ray diffraction studies of the structural organisation of prolamellar bodies isolated from Zea mays
    • W.P. Williams, E. Selstam, and T. Brain X-ray diffraction studies of the structural organisation of prolamellar bodies isolated from Zea mays FEBS Lett. 422 1998 252 254
    • (1998) FEBS Lett. , vol.422 , pp. 252-254
    • Williams, W.P.1    Selstam, E.2    Brain, T.3
  • 11
    • 0000325882 scopus 로고
    • Protection of native chlorophyll(ide) forms and of photosystem II against photodamage during early stages of chloroplast differentiation
    • F. Franck, B. Schoefs, X. Barthelemy, K.B. Mysliwa, K. Strzalka, and R. Popovic Protection of native chlorophyll(ide) forms and of photosystem II against photodamage during early stages of chloroplast differentiation Acta Physiol. Plant 17 1995 123 132
    • (1995) Acta Physiol. Plant , vol.17 , pp. 123-132
    • Franck, F.1    Schoefs, B.2    Barthelemy, X.3    Mysliwa, K.B.4    Strzalka, K.5    Popovic, R.6
  • 12
    • 0032418272 scopus 로고    scopus 로고
    • Protochlorophyllide photoreduction
    • N. Lebedev, and M.P. Timko Protochlorophyllide photoreduction Photosynth. Res. 58 1998 5 23
    • (1998) Photosynth. Res. , vol.58 , pp. 5-23
    • Lebedev, N.1    Timko, M.P.2
  • 13
    • 0033924230 scopus 로고    scopus 로고
    • Does a light-harvesting protochlorophyllide a/b-binding protein complex exist?
    • G.A. Armstrong, K. Apel, and W. Rüdiger Does a light-harvesting protochlorophyllide a/b-binding protein complex exist? Trends Plant Sci. 5 2000 40 44
    • (2000) Trends Plant Sci. , vol.5 , pp. 40-44
    • Armstrong, G.A.1    Apel, K.2    Rüdiger, W.3
  • 14
    • 0000460745 scopus 로고
    • The Shibata shift and the transformation of etioplasts to chloroplasts in wheat with clomazone fmc 57020 and amiprophos-methyl tokunol
    • N.N. Artus, M. Ryberg, A. Lindsten, H. Ryberg, and C. Sundqvist The Shibata shift and the transformation of etioplasts to chloroplasts in wheat with clomazone fmc 57020 and amiprophos-methyl tokunol Plant Physiol. 98 1992 253 263
    • (1992) Plant Physiol. , vol.98 , pp. 253-263
    • Artus, N.N.1    Ryberg, M.2    Lindsten, A.3    Ryberg, H.4    Sundqvist, C.5
  • 15
    • 0031730861 scopus 로고    scopus 로고
    • Isolation and characterization of photoactive complexes of NADPH:protochlorophyllide oxidoreductase from wheat
    • M.A. Chahdi, B. Schoefs, and F. Franck Isolation and characterization of photoactive complexes of NADPH:protochlorophyllide oxidoreductase from wheat Planta 206 1998 673 680
    • (1998) Planta , vol.206 , pp. 673-680
    • Chahdi, M.A.1    Schoefs, B.2    Franck, F.3
  • 16
    • 0036009771 scopus 로고    scopus 로고
    • Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation, and photomorphogenesis
    • H. Park, S.S. Kreunen, A.J. Cuttriss, D. DellaPenna, and B.J. Pogson Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation, and photomorphogenesis Plant Cell 14 2002 321 332
    • (2002) Plant Cell , vol.14 , pp. 321-332
    • Park, H.1    Kreunen, S.S.2    Cuttriss, A.J.3    Dellapenna, D.4    Pogson, B.J.5
  • 17
    • 0036707546 scopus 로고    scopus 로고
    • Bleaching herbicide effects on plastids of dark-grown plants: Lipid composition of etioplasts in amitrole and norflurazon-treated barley leaves
    • D. Di-Baccio, M.F. Quartacci, I. Moro, F. Dalla-Vecchia, N. La-Rocca, F.N. Rascio, and F. Navari-Izzo Bleaching herbicide effects on plastids of dark-grown plants: lipid composition of etioplasts in amitrole and norflurazon-treated barley leaves J. Exp. Bot. 53 2002 1857 1865
    • (2002) J. Exp. Bot. , vol.53 , pp. 1857-1865
    • Di-Baccio, D.1    Quartacci, M.F.2    Moro, I.3    Dalla-Vecchia, F.4    La-Rocca, N.5    Rascio, F.N.6    Navari-Izzo, F.7
  • 19
    • 0033571659 scopus 로고    scopus 로고
    • Lutein and zeaxanthin as protectors of lipid membranes against oxidative damage: The structural aspects
    • A. Sujak, J. Gabrielska, W. Grudzinski, R. Borc, P. Mazurek, and W.I. Gruszecki Lutein and zeaxanthin as protectors of lipid membranes against oxidative damage: the structural aspects Arch. Biochem. Biophys. 371 1999 301 307
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 301-307
    • Sujak, A.1    Gabrielska, J.2    Grudzinski, W.3    Borc, R.4    Mazurek, P.5    Gruszecki, W.I.6
  • 20
    • 0034284724 scopus 로고    scopus 로고
    • The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH: Protochlorophyllide oxidoreductase from Avena sativa L
    • H. Klement, U. Oster, and W. Rüdiger The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH: protochlorophyllide oxidoreductase from Avena sativa L FEBS Lett. 480 2000 306 310
    • (2000) FEBS Lett. , vol.480 , pp. 306-310
    • Klement, H.1    Oster, U.2    Rüdiger, W.3
  • 21
    • 3542996369 scopus 로고    scopus 로고
    • Surface charge densities and membrane fluidities in thylakoids with different degrees of thylakoid appression after Norflurazon treatment
    • C. Dahlin Surface charge densities and membrane fluidities in thylakoids with different degrees of thylakoid appression after Norflurazon treatment Photosynthesis 41 2003 635 639
    • (2003) Photosynthesis , vol.41 , pp. 635-639
    • Dahlin, C.1
  • 22
    • 0035981151 scopus 로고    scopus 로고
    • Carotenoid dependence of protochlorophyllide to chlorophyllide phototransformation in dark-grown wheat seedlings
    • G. Yahubyan, I. Minkov, and C. Sundqvist Carotenoid dependence of protochlorophyllide to chlorophyllide phototransformation in dark-grown wheat seedlings J. Photochem. Photobiol., B 65 2001 171 176
    • (2001) J. Photochem. Photobiol., B , vol.65 , pp. 171-176
    • Yahubyan, G.1    Minkov, I.2    Sundqvist, C.3
  • 23
    • 27444438496 scopus 로고
    • The function of carotenoids during chloroplast development: I. Effect of the herbicide SAN 9789 on chlorophyll synthesis and plastid ultrastructure
    • G. Akoyunoglou Photosynthesis V-Chloroplast Development
    • B. Klockare, L. Axelsson, H. Ryberg, A.S. Sandelius, and K.O. Widell The function of carotenoids during chloroplast development: I. Effect of the herbicide SAN 9789 on chlorophyll synthesis and plastid ultrastructure G. Akoyunoglou Photosynthesis V-Chloroplast Development Balaban Int. Sci. Serv. Philadelphia 1981 277 284
    • (1981) Balaban Int. Sci. Serv. Philadelphia , pp. 277-284
    • Klockare, B.1    Axelsson, L.2    Ryberg, H.3    Sandelius, A.S.4    Widell, K.O.5
  • 24
    • 0032055782 scopus 로고    scopus 로고
    • Carotenoids as membrane stabilizers in chloroplasts
    • M. Havaux Carotenoids as membrane stabilizers in chloroplasts Trends Plant Sci. 3 1998 147 151
    • (1998) Trends Plant Sci. , vol.3 , pp. 147-151
    • Havaux, M.1
  • 26
    • 27444435518 scopus 로고    scopus 로고
    • Membrane protein localization in non-irradiated and flash irradiated prolamellar bodies and prothylakoids, isolated from wheat, measured by fluorescence probes 1-aniline-8-naphthalene sulfonate and pyrene
    • I. Denev, and I. Minkov Membrane protein localization in non-irradiated and flash irradiated prolamellar bodies and prothylakoids, isolated from wheat, measured by fluorescence probes 1-aniline-8-naphthalene sulfonate and pyrene Bulg. J. Plant Physiol. 22 1996 40 52
    • (1996) Bulg. J. Plant Physiol. , vol.22 , pp. 40-52
    • Denev, I.1    Minkov, I.2
  • 27
    • 0030832521 scopus 로고    scopus 로고
    • Changes in the localization of the proteins in isolated inner membranes from wheat etiochloroplasts under irradiation, measured by 1-aniline-8- naphthalene sulfonate and pyrene
    • I. Denev, I. Minkov, C. Sundqvist, G. Savchenko, and E. Kluchareva Changes in the localization of the proteins in isolated inner membranes from wheat etiochloroplasts under irradiation, measured by 1-aniline-8-naphthalene sulfonate and pyrene J. Plant Physiol. 150 1997 668 673
    • (1997) J. Plant Physiol. , vol.150 , pp. 668-673
    • Denev, I.1    Minkov, I.2    Sundqvist, C.3    Savchenko, G.4    Kluchareva, E.5
  • 28
    • 0035958659 scopus 로고    scopus 로고
    • The importance of the C-terminal region and Cys residues for the membrane association of the NADPH:protochlorophyllide oxidoreductase (POR) in pea (Pisum sativum)
    • H. Aronsson, C. Sundqvist, M.P. Timko, and C. Dahlin The importance of the C-terminal region and Cys residues for the membrane association of the NADPH:protochlorophyllide oxidoreductase (POR) in pea (Pisum sativum) FEBS Lett. 502 2001 11 15
    • (2001) FEBS Lett. , vol.502 , pp. 11-15
    • Aronsson, H.1    Sundqvist, C.2    Timko, M.P.3    Dahlin, C.4
  • 29
    • 0035882551 scopus 로고    scopus 로고
    • Protochlorophyllide oxidoreductase: A homology model examined by site-directed mutagenesis
    • H.E. Townley, R.B. Sessions, A.R. Clarke, T.R. Dafforn, and W.T. Griffiths Protochlorophyllide oxidoreductase: a homology model examined by site-directed mutagenesis Proteins 44 2001 329 335
    • (2001) Proteins , vol.44 , pp. 329-335
    • Townley, H.E.1    Sessions, R.B.2    Clarke, A.R.3    Dafforn, T.R.4    Griffiths, W.T.5
  • 30
    • 0030056704 scopus 로고    scopus 로고
    • Secondary structure of NADPH:protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods
    • S.J. Birve, E. Selstam, and L.B.A. Johansson Secondary structure of NADPH:protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods Biochem. J. 317 1996 549 555
    • (1996) Biochem. J. , vol.317 , pp. 549-555
    • Birve, S.J.1    Selstam, E.2    Johansson, L.B.A.3
  • 31
    • 0020480481 scopus 로고
    • Anilinonaphtalene sulphonate as a probe of membrane composition and function
    • J. Slavik Anilinonaphtalene sulphonate as a probe of membrane composition and function Biochim. Biophys. Acta 694 1982 1 25
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 1-25
    • Slavik, J.1
  • 32
    • 0012373127 scopus 로고
    • Nuclear magnetic resonance studies of lecithin bimolecular leaflets with incorporated fluorescent probes
    • F. Podo, and J.K. Blasie Nuclear magnetic resonance studies of lecithin bimolecular leaflets with incorporated fluorescent probes Proc. Natl. Acad. Sci. U. S. A. 74 1977 1032 1036
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 1032-1036
    • Podo, F.1    Blasie, J.K.2
  • 33
    • 84981690395 scopus 로고
    • The influence of 8-hydroxyquinoline on the accumulation of porphyrins in dark-grown wheat leaves treated with 5-aminolevulinic acid
    • M. Ryberg, and C. Sundqvist The influence of 8-hydroxyquinoline on the accumulation of porphyrins in dark-grown wheat leaves treated with 5-aminolevulinic acid Physiol. Plant. 36 1976 356 361
    • (1976) Physiol. Plant. , vol.36 , pp. 356-361
    • Ryberg, M.1    Sundqvist, C.2
  • 34
    • 0018085511 scopus 로고
    • Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay
    • J.C. Bearden Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay Biochim. Biophys. Acta 533 1978 525 529
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 525-529
    • Bearden, J.C.1
  • 35
    • 0019638822 scopus 로고
    • The protochlorophyllide holochrome of barley (Hordeum vulgare L.). the effect of light on the NADPH:protochlorophyllide oxidoreductase
    • H.J. Santel, and K. Apel The protochlorophyllide holochrome of barley (Hordeum vulgare L.). The effect of light on the NADPH:protochlorophyllide oxidoreductase Eur. J. Biochem. 120 1981 95 103
    • (1981) Eur. J. Biochem. , vol.120 , pp. 95-103
    • Santel, H.J.1    Apel, K.2
  • 36
    • 84989754332 scopus 로고
    • Spectrophotometric quantitation of protochlorophyll(ide): Specific absorption and molar extinction coefficients reconsidered
    • A. Kahn Spectrophotometric quantitation of protochlorophyll(ide): specific absorption and molar extinction coefficients reconsidered Physiol. Plant. 59 1983 99 102
    • (1983) Physiol. Plant. , vol.59 , pp. 99-102
    • Kahn, A.1
  • 37
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • G. MacKinney Absorption of light by chlorophyll solutions J. Biol. Chem. 140 1941 315 322
    • (1941) J. Biol. Chem. , vol.140 , pp. 315-322
    • MacKinney, G.1
  • 38
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. the orientation factor in intramolecular energy transfer
    • R. Dale, J. Eisinger, and W. Blumberg The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer Biophys. J. 26 1979 161 194
    • (1979) Biophys. J. , vol.26 , pp. 161-194
    • Dale, R.1    Eisinger, J.2    Blumberg, W.3
  • 40
    • 0017288499 scopus 로고
    • Exposure of tryptophanil residues in proteins. Quantitative determination by fluorescence quenching studies
    • M.R. Eftink, and C.A. Ghiron Exposure of tryptophanil residues in proteins. Quantitative determination by fluorescence quenching studies Biochemistry 15 1976 672 680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 41
    • 0020026710 scopus 로고
    • A fluorescent study of a protein localization in relation to lipids in serum low density lipoproteins
    • G.E. Dobretsov, M.M. Spirin, and O.V. Chekrygin A fluorescent study of a protein localization in relation to lipids in serum low density lipoproteins Biochim. Biophys. Acta 710 1982 172 180
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 172-180
    • Dobretsov, G.E.1    Spirin, M.M.2    Chekrygin, O.V.3
  • 43
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • M.R. Eftink, and C.A. Ghiron Fluorescence quenching studies with proteins Anal. Biochem. 114 1981 199 210
    • (1981) Anal. Biochem. , vol.114 , pp. 199-210
    • Eftink, M.R.1    Ghiron, C.A.2
  • 45
    • 0001836937 scopus 로고    scopus 로고
    • Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation
    • B. Wiktorsson, M. Ryberg, and C. Sundqvist Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation Plant Physiol. Biochem. Paris 34 1 1996 23 34
    • (1996) Plant Physiol. Biochem. Paris , vol.34 , Issue.1 , pp. 23-34
    • Wiktorsson, B.1    Ryberg, M.2    Sundqvist, C.3
  • 46
    • 0032169930 scopus 로고    scopus 로고
    • The role of lipids in plastid protein transport
    • B.D. Bruce The role of lipids in plastid protein transport Plant Mol. 38 1-2 1998 223 246
    • (1998) Plant Mol. , vol.38 , Issue.1-2 , pp. 223-246
    • Bruce, B.D.1
  • 47
    • 0033063166 scopus 로고    scopus 로고
    • The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: Protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis
    • C. Dahlin, H. Aronsson, H.M. Wilks, N. Lebedev, C. Sundqvist, and M.P. Timko The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis Plant Mol. Biol. 39 2 1999 309 323
    • (1999) Plant Mol. Biol. , vol.39 , Issue.2 , pp. 309-323
    • Dahlin, C.1    Aronsson, H.2    Wilks, H.M.3    Lebedev, N.4    Sundqvist, C.5    Timko, M.P.6
  • 48
    • 0016215159 scopus 로고
    • Pyrene: A probe of lateral diffusion in the hydrophobic region of membranes
    • J.M. Vanderkooi, and J.B. Callis Pyrene: a probe of lateral diffusion in the hydrophobic region of membranes Biochemistry 13 1974 4000 4006
    • (1974) Biochemistry , vol.13 , pp. 4000-4006
    • Vanderkooi, J.M.1    Callis, J.B.2


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