메뉴 건너뛰기




Volumn 1768, Issue 9, 2007, Pages 2310-2318

Membrane curvature stress controls the maximal conversion of violaxanthin to zeaxanthin in the violaxanthin cycle-influence of α-tocopherol, cetylethers, linolenic acid, and temperature

Author keywords

Inverted hexagonal phase (HII); Membrane curvature stress; Thylakoid membrane; Violaxanthin de epoxidase (VDE); Xanthophyll cycle; Zeaxanthin

Indexed keywords

8 CETYLETHER; ALPHA TOCOPHEROL; CETYLETHER DERIVATIVE; ETHER DERIVATIVE; LINOLEIC ACID; LINOLENIC ACID; UNCLASSIFIED DRUG; VIOLAXANTHIN; ZEAXANTHIN;

EID: 34548486245     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.06.001     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 7444220226 scopus 로고    scopus 로고
    • Role of histidines in the binding of violaxanthin de-epoxidase to thylakoid membrane as studied by site-directed mutagenesis
    • Gisselsson A., Szilágyi A., and Åkerlund H.-E. Role of histidines in the binding of violaxanthin de-epoxidase to thylakoid membrane as studied by site-directed mutagenesis. Physiol. Plant. 122 (2004) 337-343
    • (2004) Physiol. Plant. , vol.122 , pp. 337-343
    • Gisselsson, A.1    Szilágyi, A.2    Åkerlund, H.-E.3
  • 2
    • 0000642171 scopus 로고
    • Photoinhibition and zeaxanthin formation in intact leaves
    • Demmig B., Winter K., Krüger A., and Czygan F.-C. Photoinhibition and zeaxanthin formation in intact leaves. Plant Physiol. 84 (1987) 218-224
    • (1987) Plant Physiol. , vol.84 , pp. 218-224
    • Demmig, B.1    Winter, K.2    Krüger, A.3    Czygan, F.-C.4
  • 3
    • 0035787269 scopus 로고    scopus 로고
    • Photosynthetic properties of an Arabidopsis thaliana mutant possessing a defective PsbS gene
    • Peterson R.B., and Havir E.A. Photosynthetic properties of an Arabidopsis thaliana mutant possessing a defective PsbS gene. Planta 214 (2001) 142-152
    • (2001) Planta , vol.214 , pp. 142-152
    • Peterson, R.B.1    Havir, E.A.2
  • 4
    • 0036030182 scopus 로고    scopus 로고
    • Structure-function analysis of photosystem II subunit S (PsbS) in vivo
    • Li X.P., Phippard A., Pasari J., and Niyogi K.K. Structure-function analysis of photosystem II subunit S (PsbS) in vivo. Funct. Plant Biol. 29 (2002) 1131-1139
    • (2002) Funct. Plant Biol. , vol.29 , pp. 1131-1139
    • Li, X.P.1    Phippard, A.2    Pasari, J.3    Niyogi, K.K.4
  • 5
    • 0001938338 scopus 로고    scopus 로고
    • The role of xanthophyll cycle carotenoids in the protection of photosynthesis
    • Demmig-Adams B., and Adams W.W. The role of xanthophyll cycle carotenoids in the protection of photosynthesis. Trends Plant Sci. 1 (1996) 21-26
    • (1996) Trends Plant Sci. , vol.1 , pp. 21-26
    • Demmig-Adams, B.1    Adams, W.W.2
  • 6
    • 0030774584 scopus 로고    scopus 로고
    • The xanthophyll cycle, its regulation and components
    • Eskling M., Arvidsson P.O., and Åkerlund H.-E. The xanthophyll cycle, its regulation and components. Physiol. Plant. 100 (1997) 806-816
    • (1997) Physiol. Plant. , vol.100 , pp. 806-816
    • Eskling, M.1    Arvidsson, P.O.2    Åkerlund, H.-E.3
  • 8
    • 0002368978 scopus 로고
    • Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching
    • Gilmore A.M., and Yamamoto H.Y. Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching. Photosynth. Res. 35 (1993) 67-78
    • (1993) Photosynth. Res. , vol.35 , pp. 67-78
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 9
    • 0016162088 scopus 로고
    • Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. III. Reaction kinetics and effect of light intensity on de-epoxidase activity and substrate availability
    • Siefermann H., and Yamamoto H.Y. Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. III. Reaction kinetics and effect of light intensity on de-epoxidase activity and substrate availability. Biochim. Biophys. Acta 357 (1974) 144-150
    • (1974) Biochim. Biophys. Acta , vol.357 , pp. 144-150
    • Siefermann, H.1    Yamamoto, H.Y.2
  • 10
    • 0016591192 scopus 로고
    • Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. IV. The effect of electron-transport conditions on violaxanthin availability
    • Siefermann H., and Yamamoto H.Y. Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. IV. The effect of electron-transport conditions on violaxanthin availability. Biochim. Biophys. Acta 387 (1975) 149-158
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 149-158
    • Siefermann, H.1    Yamamoto, H.Y.2
  • 11
    • 0037044837 scopus 로고    scopus 로고
    • Molecular configuration of xanthophyll cycle carotenoids in photosystem II antenna complexes
    • Ruban A.V., Pascal A., Lee P.J., Robert B., and Horton P. Molecular configuration of xanthophyll cycle carotenoids in photosystem II antenna complexes. J. Biol. Chem. 277 (2002) 42937-42942
    • (2002) J. Biol. Chem. , vol.277 , pp. 42937-42942
    • Ruban, A.V.1    Pascal, A.2    Lee, P.J.3    Robert, B.4    Horton, P.5
  • 12
    • 0035933719 scopus 로고    scopus 로고
    • De-epoxidation of violaxanthin after reconstitution into different carotenoid binding sites of light-harvesting complex II
    • Jahns P., Wehner A., Paulsen H., and Hobe S. De-epoxidation of violaxanthin after reconstitution into different carotenoid binding sites of light-harvesting complex II. J. Biol. Chem. 276 (2001) 22154-22159
    • (2001) J. Biol. Chem. , vol.276 , pp. 22154-22159
    • Jahns, P.1    Wehner, A.2    Paulsen, H.3    Hobe, S.4
  • 13
    • 0032816979 scopus 로고    scopus 로고
    • Xanthophyll cycle pigment localization and dynamics during exposure to low temperatures and light stress in Vinca major
    • Verhoeven A.S., Adams W.W., Demmig-Adams B., Croce R., and Bassi R. Xanthophyll cycle pigment localization and dynamics during exposure to low temperatures and light stress in Vinca major. Plant Physiol. 120 (1999) 727-738
    • (1999) Plant Physiol. , vol.120 , pp. 727-738
    • Verhoeven, A.S.1    Adams, W.W.2    Demmig-Adams, B.3    Croce, R.4    Bassi, R.5
  • 14
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu Z., Yan H., Kuang T., Zhang J., Gui L., An X., and Chang W. Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 428 (2004) 287-292
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Kuang, T.3    Zhang, J.4    Gui, L.5    An, X.6    Chang, W.7
  • 15
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
    • Standfuss R., van Scheltinga A.C.T., Lamborghini M., and Kuhlbrandt W. Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J. 24 (2005) 919-928
    • (2005) EMBO J. , vol.24 , pp. 919-928
    • Standfuss, R.1    van Scheltinga, A.C.T.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 16
    • 0033569933 scopus 로고    scopus 로고
    • Carotenoid-binding sites of the major light-harvesting complex II of higher plants
    • Croce R., Weiss S., and Bassi R. Carotenoid-binding sites of the major light-harvesting complex II of higher plants. J. Biol. Chem. 274 (1999) 29613-29623
    • (1999) J. Biol. Chem. , vol.274 , pp. 29613-29623
    • Croce, R.1    Weiss, S.2    Bassi, R.3
  • 17
    • 0028005184 scopus 로고
    • The effects of illumination on the xanthophyll composition of the photosystem-II light harvesting complexes of spinach thylakoid membranes
    • Ruban A.V., Young A.J., Pascal A.A., and Horton P. The effects of illumination on the xanthophyll composition of the photosystem-II light harvesting complexes of spinach thylakoid membranes. Plant Physiol. 104 (1994) 227-234
    • (1994) Plant Physiol. , vol.104 , pp. 227-234
    • Ruban, A.V.1    Young, A.J.2    Pascal, A.A.3    Horton, P.4
  • 18
    • 0031669979 scopus 로고    scopus 로고
    • Time course of changes in the quantities of violaxanthin de-epoxidase, xanthophylls and ascorbate in spinach upon shift from low to high light
    • Eskling M., and Åkerlund H.-E. Time course of changes in the quantities of violaxanthin de-epoxidase, xanthophylls and ascorbate in spinach upon shift from low to high light. Photosynth. Res. 57 (1998) 41-50
    • (1998) Photosynth. Res. , vol.57 , pp. 41-50
    • Eskling, M.1    Åkerlund, H.-E.2
  • 19
    • 0030812109 scopus 로고    scopus 로고
    • Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes
    • Arvidsson P.O., Carlsson M., Steffánsson H., Albertsson P.Å., and Åkerlund H.-E. Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes. Photosynth. Res. 52 (1997) 39-48
    • (1997) Photosynth. Res. , vol.52 , pp. 39-48
    • Arvidsson, P.O.1    Carlsson, M.2    Steffánsson, H.3    Albertsson, P.Å.4    Åkerlund, H.-E.5
  • 20
    • 0036380814 scopus 로고    scopus 로고
    • Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers
    • Latowski D., Kruk J., Burda K., Skrzynecka-Jaskier M., Kostecka-Gugala A., and Strzalka K. Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers. Eur. J. Biochem. 269 (2002) 4656-4665
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4656-4665
    • Latowski, D.1    Kruk, J.2    Burda, K.3    Skrzynecka-Jaskier, M.4    Kostecka-Gugala, A.5    Strzalka, K.6
  • 21
    • 0031588952 scopus 로고    scopus 로고
    • Purification and properties of violaxanthin de-epoxidase from spinach
    • Havir E.A., Tausta S.L., and Peterson R.B. Purification and properties of violaxanthin de-epoxidase from spinach. Plant Sci. 123 (1997) 57-66
    • (1997) Plant Sci. , vol.123 , pp. 57-66
    • Havir, E.A.1    Tausta, S.L.2    Peterson, R.B.3
  • 22
    • 0018129919 scopus 로고
    • Violaxanthin de-epoxidase-Lipid composition and substrate specificity
    • Yamamoto H.Y., and Higashi R.M. Violaxanthin de-epoxidase-Lipid composition and substrate specificity. Arch. Biochem. Biophys. 190 (1978) 514-522
    • (1978) Arch. Biochem. Biophys. , vol.190 , pp. 514-522
    • Yamamoto, H.Y.1    Higashi, R.M.2
  • 23
    • 2942700872 scopus 로고    scopus 로고
    • Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity
    • Latowski D., Åkerlund H.-E., and Strzalka K. Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. Biochemistry 43 (2004) 4417-4420
    • (2004) Biochemistry , vol.43 , pp. 4417-4420
    • Latowski, D.1    Åkerlund, H.-E.2    Strzalka, K.3
  • 24
    • 33746931213 scopus 로고    scopus 로고
    • Functional roles of the major chloroplast lipids in the violaxanthin cycle
    • Yamamoto H.Y. Functional roles of the major chloroplast lipids in the violaxanthin cycle. Planta 224 (2006) 719-724
    • (2006) Planta , vol.224 , pp. 719-724
    • Yamamoto, H.Y.1
  • 25
    • 0018245715 scopus 로고
    • Plant lipids and their role in membrane-function
    • Quinn P.J., and Williams W.P. Plant lipids and their role in membrane-function. Prog. Biophys. Mol. Biol. 34 (1978) 109-173
    • (1978) Prog. Biophys. Mol. Biol. , vol.34 , pp. 109-173
    • Quinn, P.J.1    Williams, W.P.2
  • 26
    • 0002195611 scopus 로고
    • Chloroplast lipids and the assembly of membranes
    • Sudnqvist C., and Rydberg M. (Eds), Academic Press. 0-12-676960-5
    • Selstam E., and Wigge A.W. Chloroplast lipids and the assembly of membranes. In: Sudnqvist C., and Rydberg M. (Eds). Pigment-Protein Complexes in Plastids - Synthesis and Assembly (1993), Academic Press. 0-12-676960-5 241-277
    • (1993) Pigment-Protein Complexes in Plastids - Synthesis and Assembly , pp. 241-277
    • Selstam, E.1    Wigge, A.W.2
  • 27
    • 0027518957 scopus 로고
    • Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes
    • Gibson N.J., and Brown M.F. Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes. Biochemistry 32 (1993) 2438-2454
    • (1993) Biochemistry , vol.32 , pp. 2438-2454
    • Gibson, N.J.1    Brown, M.F.2
  • 28
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by non-lamellar-forming lipids
    • Botelho A.V., Gibson N.J., Thurmond R.L., Wang Y., and Brown M.F. Conformational energetics of rhodopsin modulated by non-lamellar-forming lipids. Biochemistry 41 (2002) 6354-6368
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Botelho, A.V.1    Gibson, N.J.2    Thurmond, R.L.3    Wang, Y.4    Brown, M.F.5
  • 30
    • 0032404028 scopus 로고    scopus 로고
    • Enhancement of phosphoinositide 3-kinase (PI 3-kinase) activity by membrane curvature and inositol-phospholipid-binding peptides
    • Hubner S., Couvillon A.D., Kas J.A., Bankaitis V.A., Vegners R., Carpenter C.L., and Janmey P.A. Enhancement of phosphoinositide 3-kinase (PI 3-kinase) activity by membrane curvature and inositol-phospholipid-binding peptides. Eur. J. Biochem. 258 (1998) 846-853
    • (1998) Eur. J. Biochem. , vol.258 , pp. 846-853
    • Hubner, S.1    Couvillon, A.D.2    Kas, J.A.3    Bankaitis, V.A.4    Vegners, R.5    Carpenter, C.L.6    Janmey, P.A.7
  • 31
    • 0037136071 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidyltransferase and protein kinase C recognize different physical features of membranes: differential responses to an oxidized phosphatidylcholine
    • Drobnies A.E., Davies S.M.A., Kraayenhof R., Epand R.F., Epand R.M., and Cornall R.B. CTP:phosphocholine cytidyltransferase and protein kinase C recognize different physical features of membranes: differential responses to an oxidized phosphatidylcholine. Biochim. Biophys. Acta-Biomemb. 1564 (2002) 82-90
    • (2002) Biochim. Biophys. Acta-Biomemb. , vol.1564 , pp. 82-90
    • Drobnies, A.E.1    Davies, S.M.A.2    Kraayenhof, R.3    Epand, R.F.4    Epand, R.M.5    Cornall, R.B.6
  • 32
    • 0036418141 scopus 로고    scopus 로고
    • The chequered history of the development and use of simultaneous equations for the accurate determination of chlorophylls a and b
    • Porra R.J. The chequered history of the development and use of simultaneous equations for the accurate determination of chlorophylls a and b. Photosynth. Res. 73 (2002) 149-156
    • (2002) Photosynth. Res. , vol.73 , pp. 149-156
    • Porra, R.J.1
  • 33
    • 0000959808 scopus 로고
    • Leaf xanthophyll content and composition in sun and shade determined by HPLC
    • Thayer S.S., and Björkman O. Leaf xanthophyll content and composition in sun and shade determined by HPLC. Photosynth. Res. 23 (1990) 331-343
    • (1990) Photosynth. Res. , vol.23 , pp. 331-343
    • Thayer, S.S.1    Björkman, O.2
  • 34
    • 0141706805 scopus 로고    scopus 로고
    • Effects of unsaturated fatty acids and triacylglycerols on phosphatidylethanolamine membrane structure
    • Prades J., Funari S.S., Escribá P.V., and Barceló F. Effects of unsaturated fatty acids and triacylglycerols on phosphatidylethanolamine membrane structure. J. Lipid Res. 44 (2003) 1720-1727
    • (2003) J. Lipid Res. , vol.44 , pp. 1720-1727
    • Prades, J.1    Funari, S.S.2    Escribá, P.V.3    Barceló, F.4
  • 35
    • 0027227672 scopus 로고
    • LHCII, the major light-harvesting pigment-protein complex is a zeaxanthin-epoxidase
    • Gruszecki W.I., and Krupa Z. LHCII, the major light-harvesting pigment-protein complex is a zeaxanthin-epoxidase. Biochim. Biophys. Acta 1144 (1993) 97-101
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 97-101
    • Gruszecki, W.I.1    Krupa, Z.2
  • 36
    • 0019329482 scopus 로고
    • The fluidity of chloroplast thylakoid membranes and their constituent lipids-A comparative-study by electron-spin-resonance
    • Hiller R.G., and Raison J.K. The fluidity of chloroplast thylakoid membranes and their constituent lipids-A comparative-study by electron-spin-resonance. Biochim. Biophys. Acta 599 (1980) 63-72
    • (1980) Biochim. Biophys. Acta , vol.599 , pp. 63-72
    • Hiller, R.G.1    Raison, J.K.2
  • 37
    • 0023052455 scopus 로고
    • Metabolic changes of membrane lipid composition in Acholeplasma laidlawii by hydrocarbons, alcohols and detergents: arguments for effects on lipid packing
    • Wieslander Å., Rilfors L., and Lindblom G. Metabolic changes of membrane lipid composition in Acholeplasma laidlawii by hydrocarbons, alcohols and detergents: arguments for effects on lipid packing. Biochemistry 25 (1986) 7511-7517
    • (1986) Biochemistry , vol.25 , pp. 7511-7517
    • Wieslander, Å.1    Rilfors, L.2    Lindblom, G.3
  • 38
    • 0036166427 scopus 로고    scopus 로고
    • The function of tocopherols and tocotrienols in plants
    • Munne-Bosch S., and Alegre L. The function of tocopherols and tocotrienols in plants. Crit. Rev. Plant Sci. 21 (2002) 31-57
    • (2002) Crit. Rev. Plant Sci. , vol.21 , pp. 31-57
    • Munne-Bosch, S.1    Alegre, L.2
  • 39
    • 0033829613 scopus 로고    scopus 로고
    • Photodamage of the photosynthetic apparatus and its dependence on the leaf development as stage in the npq1 Arabidopsis mutant deficient in the xanthophyll cycle enzyme violaxanthin de-epoxidase
    • Havaux M., Bonfils J.-P., Lütz C., and Niyogi K.K. Photodamage of the photosynthetic apparatus and its dependence on the leaf development as stage in the npq1 Arabidopsis mutant deficient in the xanthophyll cycle enzyme violaxanthin de-epoxidase. Plant Physiol. 124 (2000) 273-284
    • (2000) Plant Physiol. , vol.124 , pp. 273-284
    • Havaux, M.1    Bonfils, J.-P.2    Lütz, C.3    Niyogi, K.K.4
  • 40
    • 0032545804 scopus 로고    scopus 로고
    • Effects of polar carotenoids on the shape of the hydrophobic barrier of phospholipid bilayers
    • Wisniewska A., and Subczynski W.K. Effects of polar carotenoids on the shape of the hydrophobic barrier of phospholipid bilayers. Biochim. Biophys. Acta 1368 (2006) 235-246
    • (2006) Biochim. Biophys. Acta , vol.1368 , pp. 235-246
    • Wisniewska, A.1    Subczynski, W.K.2
  • 41
    • 0019875686 scopus 로고
    • Formation of inverted micelles in dispersions of mixed galactolipids
    • Sen A., Williams W.P., Brain A.P.R., Dickens M.J., and Quinn P.J. Formation of inverted micelles in dispersions of mixed galactolipids. Nature 293 (1981) 488-490
    • (1981) Nature , vol.293 , pp. 488-490
    • Sen, A.1    Williams, W.P.2    Brain, A.P.R.3    Dickens, M.J.4    Quinn, P.J.5
  • 42
    • 0010462322 scopus 로고
    • 32P-NMR observation of the temperature and glycerol induced non-lamellar phase formation in wheat thylakoid membranes
    • 32P-NMR observation of the temperature and glycerol induced non-lamellar phase formation in wheat thylakoid membranes. J. Biol. Phys. 21 (1995) 125-139
    • (1995) J. Biol. Phys. , vol.21 , pp. 125-139
    • Haraczyk, K.1    Strzalka, K.2    Dietrich, W.3    Blicharski, J.S.4
  • 43
    • 33845389746 scopus 로고    scopus 로고
    • Lipid dependence of diadinoxanthin solubilization and de-epoxidation in artificial membrane systems resembling the lipid composition of the natural thylakoid membrane
    • Goss R., Latowski D., Grzyb J., Vieler A., Lohr M., Wilhelm C., and Strzalka K. Lipid dependence of diadinoxanthin solubilization and de-epoxidation in artificial membrane systems resembling the lipid composition of the natural thylakoid membrane. Biochim. Biophys. Acta 1768 (2007) 67-75
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 67-75
    • Goss, R.1    Latowski, D.2    Grzyb, J.3    Vieler, A.4    Lohr, M.5    Wilhelm, C.6    Strzalka, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.