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Volumn 214, Issue 3, 2002, Pages 476-483

Overexpression of violaxanthin de-epoxidase: Properties of C-terminal deletions on activity and pH-dependent lipid binding

Author keywords

Lipocalin; Nicotiana (violaxanthin de epoxidase); Non photochemical quenching; Violaxanthin de epoxidase; Xanthophyll cycle

Indexed keywords

AMINO ACIDS; CATALYSIS; ESCHERICHIA COLI; LIPIDS; PH EFFECTS; PROTEINS; TOBACCO;

EID: 0036935115     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-001-0704-2     Document Type: Article
Times cited : (41)

References (55)
  • 1
    • 0030471854 scopus 로고    scopus 로고
    • Purification and identification of the violaxanthin deepoxidase as a 43 kDa protein
    • Arvidsson P-O, Bratt CE, Carlsson M, Åkerlund H-E (1996) Purification and identification of the violaxanthin deepoxidase as a 43 kDa protein. Photosynth Res 49:119-129
    • (1996) Photosynth Res , vol.49 , pp. 119-129
    • Arvidsson, P.-O.1    Bratt, C.E.2    Carlsson, M.3    Åkerlund, H.-E.4
  • 2
    • 0029842720 scopus 로고    scopus 로고
    • Xanthophyll biosynthesis: Cloning, expression, functional reconstitution, and regulation of β-cyclohexenyl carotenoid epoxidase from pepper (Capsicum annuum)
    • Bouvier F, d'Harlingue A, Hugueney P, Marin E, Marion-Poll A, Camara B (1996) Xanthophyll biosynthesis: Cloning, expression, functional reconstitution, and regulation of β-cyclohexenyl carotenoid epoxidase from pepper (Capsicum annuum). J Biol Chem 271:28861-28867
    • (1996) J Biol Chem , vol.271 , pp. 28861-28867
    • Bouvier, F.1    D'Harlingue, A.2    Hugueney, P.3    Marin, E.4    Marion-Poll, A.5    Camara, B.6
  • 3
    • 34249758236 scopus 로고
    • Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration
    • Bratt CE, Arvidsson P-O, Carlsson M, Åkerlund H-E (1995) Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration. Photosynth Res 45:169-175
    • (1995) Photosynth Res , vol.45 , pp. 169-175
    • Bratt, C.E.1    Arvidsson, P.-O.2    Carlsson, M.3    Åkerlund, H.-E.4
  • 4
    • 0024825088 scopus 로고
    • High level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann U, Mattes RE, Buckel P (1989) High level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85:109-114
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 5
    • 0030011229 scopus 로고    scopus 로고
    • Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli
    • Bugos RC, Yamamoto HY (1996) Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli. Proc Natl Acad Sci USA 93:6320-6325
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6320-6325
    • Bugos, R.C.1    Yamamoto, H.Y.2
  • 6
    • 0032546960 scopus 로고    scopus 로고
    • Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants
    • Bugos RC, Hieber AD, Yamamoto HY (1998) Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J Biol Chem 273:15321-15324
    • (1998) J Biol Chem , vol.273 , pp. 15321-15324
    • Bugos, R.C.1    Hieber, A.D.2    Yamamoto, H.Y.3
  • 7
    • 0033199273 scopus 로고    scopus 로고
    • Developmental expression of violaxanthin de-epoxidase in leaves of tobacco growing under high and low light
    • Bugos RC, Chang S-H, Yamamoto HY (1999) Developmental expression of violaxanthin de-epoxidase in leaves of tobacco growing under high and low light. Plant Physiol 121:207-213
    • (1999) Plant Physiol , vol.121 , pp. 207-213
    • Bugos, R.C.1    Chang, S.-H.2    Yamamoto, H.Y.3
  • 8
    • 0030697850 scopus 로고    scopus 로고
    • Structure and expression of a cDNA encoding zeaxanthin epoxidase, isolated from a wilt-related tomato (Lycopersicon esculentum Mill.) library
    • Burbidge A, Grieve T, Terry C, Corlett J, Thompson A, Taylor I (1997) Structure and expression of a cDNA encoding zeaxanthin epoxidase, isolated from a wilt-related tomato (Lycopersicon esculentum Mill.) library. J Exp Bot 48:1749-1750
    • (1997) J Exp Bot , vol.48 , pp. 1749-1750
    • Burbidge, A.1    Grieve, T.2    Terry, C.3    Corlett, J.4    Thompson, A.5    Taylor, I.6
  • 9
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase
    • Chaddock AM, Mant A, Karnauchov I, Brink S, Herrmann RG, Klosgen RB, Robinson C (1995) A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase. EMBO J 14:2715-2722
    • (1995) EMBO J , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchov, I.3    Brink, S.4    Herrmann, R.G.5    Klosgen, R.B.6    Robinson, C.7
  • 10
    • 0001476137 scopus 로고    scopus 로고
    • Antisense suppression of violaxanthin de-epoxidase in tobacco does not affect plant performance in controlled growth conditions
    • Chang S-H, Bugos RC, Sun W-H, Yamamoto HY (2000) Antisense suppression of violaxanthin de-epoxidase in tobacco does not affect plant performance in controlled growth conditions. Photosynth Res 64:95-103
    • (2000) Photosynth Res , vol.64 , pp. 95-103
    • Chang, S.-H.1    Bugos, R.C.2    Sun, W.-H.3    Yamamoto, H.Y.4
  • 11
    • 0027140797 scopus 로고
    • Improved high-level constitutive foreign gene expression in plants using an AMV RNA4 untranslated leader sequence
    • Datla RSS, Bekkaoui F, Hammerlindl JK, Pilate G, Dunstan DI, Crosby WL (1993) Improved high-level constitutive foreign gene expression in plants using an AMV RNA4 untranslated leader sequence. Plant Sci 94:139-149
    • (1993) Plant Sci , vol.94 , pp. 139-149
    • Datla, R.S.S.1    Bekkaoui, F.2    Hammerlindl, J.K.3    Pilate, G.4    Dunstan, D.I.5    Crosby, W.L.6
  • 12
    • 0000642171 scopus 로고
    • Photoinhibition and zeaxanthin formation in intact leaves. A possible role of the xanthophyll cycle in the dissipation of excess light energy
    • Demmig B, Winter K, Krüger A, Czygan F-C (1987) Photoinhibition and zeaxanthin formation in intact leaves. A possible role of the xanthophyll cycle in the dissipation of excess light energy. Plant Physiol 84:218-224
    • (1987) Plant Physiol , vol.84 , pp. 218-224
    • Demmig, B.1    Winter, K.2    Krüger, A.3    Czygan, F.-C.4
  • 13
    • 51249162971 scopus 로고
    • Rapid, efficient production of homozygous transgenic tobacco plants with Agrobacterium tumefaciens: A seed-to-seed protocol
    • Fisher DK, Guiltinan MJ (1995) Rapid, efficient production of homozygous transgenic tobacco plants with Agrobacterium tumefaciens: A seed-to-seed protocol. Plant Mol Biol Rep 13:278-289
    • (1995) Plant Mol Biol Rep , vol.13 , pp. 278-289
    • Fisher, D.K.1    Guiltinan, M.J.2
  • 14
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower DR (1996) The lipocalin protein family: Structure and function. Biochem J 318:1-14
    • (1996) Biochem J , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 15
    • 0025869235 scopus 로고
    • 18 high-performance liquid chromatographic column
    • 18 high-performance liquid chromatographic column. J Chromatogr 543:137-145
    • (1991) J Chromatogr , vol.543 , pp. 137-145
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 16
    • 0026544131 scopus 로고
    • Dark induction of zeaxanthin-dependent nonphotochemical fluorescence quenching mediated by ATP
    • Gilmore AM, Yamamoto HY (1992) Dark induction of zeaxanthin-dependent nonphotochemical fluorescence quenching mediated by ATP. Proc Natl Acad Sci USA 89:1899-1903
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1899-1903
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 17
    • 0002368978 scopus 로고
    • Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthinindependent quenching
    • Gilmore AM, Yamamoto HY (1993) Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthinindependent quenching. Photosynth Res 35:67-78
    • (1993) Photosynth Res , vol.35 , pp. 67-78
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 18
    • 0028953463 scopus 로고
    • Xanthophyll cycledependent quenching of photosystem II chlorophyll a fluorescence: Formation of a quenching complex with a short fluorescence lifetime
    • Gilmore AM, Hazlett TL, Govindjee (1995) Xanthophyll cycledependent quenching of photosystem II chlorophyll a fluorescence: Formation of a quenching complex with a short fluorescence lifetime. Proc Natl Acad Sci USA 92:2273-2277
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2273-2277
    • Gilmore, A.M.1    Hazlett, T.L.2    Govindjee3
  • 19
    • 0029861283 scopus 로고    scopus 로고
    • Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: Photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence
    • Gilmore AM, Hazlett TL, Debrunner PG, Govindjee (1996) Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: Photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence. Photosynth Res 48:171-187
    • (1996) Photosynth Res , vol.48 , pp. 171-187
    • Gilmore, A.M.1    Hazlett, T.L.2    Debrunner, P.G.3    Govindjee4
  • 20
    • 48749149469 scopus 로고
    • Monogalactosyldiacylglycerol: The most abundant polar lipid in nature
    • Gounaris K, Barber J (1983) Monogalactosyldiacylglycerol: The most abundant polar lipid in nature. Trends Biochem Sci 8:378-381
    • (1983) Trends Biochem Sci , vol.8 , pp. 378-381
    • Gounaris, K.1    Barber, J.2
  • 21
    • 77956981332 scopus 로고
    • Photosynthesis and light activation of ribulose 1,5-bisphosphate carboxylase in the presence of starch
    • Grub A, Mächler F (1990) Photosynthesis and light activation of ribulose 1,5-bisphosphate carboxylase in the presence of starch. J Exp Bot 41:1293-1302
    • (1990) J Exp Bot , vol.41 , pp. 1293-1302
    • Grub, A.1    Mächler, F.2
  • 22
    • 0001227304 scopus 로고
    • Lichtbedingte pH-erniedrigung in einem chloroplasten-kompartiment als ursache der enzymatischen violaxanthin- → zeaxanthin-umwandlung; beziehungen zur photophosphorylierung
    • Hager A (1969) Lichtbedingte pH-erniedrigung in einem chloroplasten-kompartiment als ursache der enzymatischen violaxanthin- → zeaxanthin-umwandlung; beziehungen zur photophosphorylierung. Planta 89:224-243
    • (1969) Planta , vol.89 , pp. 224-243
    • Hager, A.1
  • 23
    • 85006828126 scopus 로고
    • Die reversiblen, lichtabhängigen xanthophyllumwandlungen im chloroplasten
    • Hager A (1975) Die reversiblen, lichtabhängigen xanthophyllumwandlungen im chloroplasten. Ber Dtsch Bot Ges 88:27-44
    • (1975) Ber Dtsch Bot Ges , vol.88 , pp. 27-44
    • Hager, A.1
  • 24
    • 0028004703 scopus 로고
    • Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
    • Hager A, Holocher K (1994) Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease. Planta 192:581-589
    • (1994) Planta , vol.192 , pp. 581-589
    • Hager, A.1    Holocher, K.2
  • 25
    • 0031588952 scopus 로고    scopus 로고
    • Purification and properties of violaxanthin de-epoxidase from spinach
    • Havir EA, Tausta SL, Peterson RB (1997) Purification and properties of violaxanthin de-epoxidase from spinach. Plant Sci 123:57-66
    • (1997) Plant Sci , vol.123 , pp. 57-66
    • Havir, E.A.1    Tausta, S.L.2    Peterson, R.B.3
  • 26
    • 0030589641 scopus 로고    scopus 로고
    • High level expression of Ricinus communis casbene synthase gene in Escherichia coli and characterization of recombinant enzyme
    • Hill AM, Cane DE, Mau CJD, West CA (1996) High level expression of Ricinus communis casbene synthase gene in Escherichia coli and characterization of recombinant enzyme. Arch Biochem Biophys 336:283-289
    • (1996) Arch Biochem Biophys , vol.336 , pp. 283-289
    • Hill, A.M.1    Cane, D.E.2    Mau, C.J.D.3    West, C.A.4
  • 28
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • Hynds PJ, Robinson D, Robinson C (1998) The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J Biol Chem 273:34868-34874
    • (1998) J Biol Chem , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 29
    • 0030698668 scopus 로고    scopus 로고
    • Yeast acetyl-CoA carboxylase is associated with the cytoplasmic surface of the endoplasmic reticulum
    • Ivessa AS, Schneiter R, Kohlwein SD (1997) Yeast acetyl-CoA carboxylase is associated with the cytoplasmic surface of the endoplasmic reticulum. Eur J Cell Biol 74:399-406
    • (1997) Eur J Cell Biol , vol.74 , pp. 399-406
    • Ivessa, A.S.1    Schneiter, R.2    Kohlwein, S.D.3
  • 30
    • 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
  • 31
    • 0012382569 scopus 로고
    • Solubilization of ribulose-1,5-bisphosphate carboxylase from the membrane fraction of pea leaves
    • Makino A, Osmond B (1991) Solubilization of ribulose-1,5-bisphosphate carboxylase from the membrane fraction of pea leaves. Photosynth Res 29:79-86
    • (1991) Photosynth Res , vol.29 , pp. 79-86
    • Makino, A.1    Osmond, B.2
  • 32
    • 0029873984 scopus 로고    scopus 로고
    • Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana
    • Marin E, Nussaume L, Quesada A, Gonneau M, Sotta B, Hugueney P, Frey A, Marion-Poll A (1996) Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana. EMBO J 15:2331-2342
    • (1996) EMBO J , vol.15 , pp. 2331-2342
    • Marin, E.1    Nussaume, L.2    Quesada, A.3    Gonneau, M.4    Sotta, B.5    Hugueney, P.6    Frey, A.7    Marion-Poll, A.8
  • 33
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bio assays with tobacco tissue cultures
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bio assays with tobacco tissue cultures. Physiol Plant 15:473-497
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 34
    • 0032125062 scopus 로고    scopus 로고
    • Arabidopsis mutants define a central role for the xanthophyll cycle in the regulation of photosynthetic energy conversion
    • Niyogi KK, Grossman AR, Björkman O (1998) Arabidopsis mutants define a central role for the xanthophyll cycle in the regulation of photosynthetic energy conversion. Plant Cell 10:1121-1134
    • (1998) Plant Cell , vol.10 , pp. 1121-1134
    • Niyogi, K.K.1    Grossman, A.R.2    Björkman, O.3
  • 35
    • 0035142771 scopus 로고    scopus 로고
    • When there is too much light
    • Ort DR (2001) When there is too much light. Plant Physiol 125:29-32
    • (2001) Plant Physiol , vol.125 , pp. 29-32
    • Ort, D.R.1
  • 36
    • 0021876620 scopus 로고
    • Homology of β-lactoglobulin, serum retinol binding protein and protein HC
    • Pervaiz S, Brew K (1985) Homology of β-lactoglobulin, serum retinol binding protein and protein HC. Science 228:335-337
    • (1985) Science , vol.228 , pp. 335-337
    • Pervaiz, S.1    Brew, K.2
  • 37
    • 0023609533 scopus 로고
    • 1-acid glycoprotein and serum retinol binding protein and its relatives
    • 1-acid glycoprotein and serum retinol binding protein and its relatives. FASEB J 1:209-214
    • (1987) FASEB J , vol.1 , pp. 209-214
    • Pervaiz, S.1    Brew, K.2
  • 38
    • 0032169929 scopus 로고    scopus 로고
    • Multiple pathways for the targeting of thylakoid proteins in chloroplasts
    • Robinson C, Hynds PJ, Robinson D, Mant A (1998) Multiple pathways for the targeting of thylakoid proteins in chloroplasts. Plant Mol Biol 38:209-221
    • (1998) Plant Mol Biol , vol.38 , pp. 209-221
    • Robinson, C.1    Hynds, P.J.2    Robinson, D.3    Mant, A.4
  • 39
    • 0030060496 scopus 로고    scopus 로고
    • Violaxanthin de-epoxidase: Purification of a 43-kilodalton lumenal protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride
    • Rockholm DC, Yamamoto HY (1996) Violaxanthin de-epoxidase: Purification of a 43-kilodalton lumenal protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride. Plant Physiol 110:697-703
    • (1996) Plant Physiol , vol.110 , pp. 697-703
    • Rockholm, D.C.1    Yamamoto, H.Y.2
  • 41
    • 0030026850 scopus 로고    scopus 로고
    • Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
    • Schlicher T, Soll J (1996) Molecular chaperones are present in the thylakoid lumen of pea chloroplasts. FEBS Lett 379:302-304
    • (1996) FEBS Lett , vol.379 , pp. 302-304
    • Schlicher, T.1    Soll, J.2
  • 42
    • 34250126784 scopus 로고
    • Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer
    • Schreiber U, Schliwa U, Bilger W (1986) Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer. Photosynth Res 10:51-62
    • (1986) Photosynth Res , vol.10 , pp. 51-62
    • Schreiber, U.1    Schliwa, U.2    Bilger, W.3
  • 43
    • 0016685138 scopus 로고
    • Properties of NADPH and oxygen-dependent zeaxanthin epoxidation in isolated chloroplasts. A transmembrane model for the violaxanthin cycle
    • Siefermann D, Yamamoto HY (1975) Properties of NADPH and oxygen-dependent zeaxanthin epoxidation in isolated chloroplasts. A transmembrane model for the violaxanthin cycle. Arch Biochem Biophys 171:70-77
    • (1975) Arch Biochem Biophys , vol.171 , pp. 70-77
    • Siefermann, D.1    Yamamoto, H.Y.2
  • 45
    • 0034961322 scopus 로고    scopus 로고
    • Suppression of zeaxanthin formation does not reduce photosynthesis and growth of transgenic tobacco under field conditions
    • Sun W-H, Verhoeven AS, Bugos RC, Yamamoto HY (2001) Suppression of zeaxanthin formation does not reduce photosynthesis and growth of transgenic tobacco under field conditions. Photosynth Res 67:41-50
    • (2001) Photosynth Res , vol.67 , pp. 41-50
    • Sun, W.-H.1    Verhoeven, A.S.2    Bugos, R.C.3    Yamamoto, H.Y.4
  • 46
    • 0027173978 scopus 로고
    • Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ
    • Süss K-H, Arkona C, Manteuffel R, Adler K (1993) Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proc Natl Acad Sci USA 90:5514-5518
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5514-5518
    • Süss, K.-H.1    Arkona, C.2    Manteuffel, R.3    Adler, K.4
  • 47
    • 34249958267 scopus 로고
    • The use of chlorophyll fluorescence nomenclature in plant stress physiology
    • van Kooten O, Snel JFH (1990) The use of chlorophyll fluorescence nomenclature in plant stress physiology. Photosynth Res 25:147-150
    • (1990) Photosynth Res , vol.25 , pp. 147-150
    • Van Kooten, O.1    Snel, J.F.H.2
  • 48
    • 0034950821 scopus 로고    scopus 로고
    • Transgenic tobacco with suppressed zeaxanthin formation is susceptible to stress-induced photoinhibition
    • Verhoeven AS, Bugos RC, Yamamoto HY (2001) Transgenic tobacco with suppressed zeaxanthin formation is susceptible to stress-induced photoinhibition. Photosynth Res 67:27-39
    • (2001) Photosynth Res , vol.67 , pp. 27-39
    • Verhoeven, A.S.1    Bugos, R.C.2    Yamamoto, H.Y.3
  • 49
    • 0000823149 scopus 로고
    • Salt-mediated interactions between vesicles of the thylakoid lipid digalactosyldiacylglycerol
    • Webb MS, Tilcock CPS, Green BR (1988) Salt-mediated interactions between vesicles of the thylakoid lipid digalactosyldiacylglycerol. Biochim Biophys Acta 938:323-333
    • (1988) Biochim Biophys Acta , vol.938 , pp. 323-333
    • Webb, M.S.1    Tilcock, C.P.S.2    Green, B.R.3
  • 50
    • 0031105805 scopus 로고    scopus 로고
    • Expression of the Arabidopsis G-protein Gpα1: Purification and characterization of the recombinant protein
    • Wise A, Thomas PG, Carr TH, Murphy GA, Millner PA (1997) Expression of the Arabidopsis G-protein Gpα1: Purification and characterization of the recombinant protein. Plant Mol Biol 33:723-728
    • (1997) Plant Mol Biol , vol.33 , pp. 723-728
    • Wise, A.1    Thomas, P.G.2    Carr, T.H.3    Murphy, G.A.4    Millner, P.A.5
  • 51
    • 0000171640 scopus 로고
    • Xanthophyll cycles
    • Yamamoto HY (1985) Xanthophyll cycles. Methods Enzymol 110:303-312
    • (1985) Methods Enzymol , vol.110 , pp. 303-312
    • Yamamoto, H.Y.1
  • 52
    • 0018129919 scopus 로고
    • Violaxanthin de-epoxidase. Lipid composition and substrate specificity
    • Yamamoto HY, Higashi RM (1978) Violaxanthin de-epoxidase. Lipid composition and substrate specificity. Arch Biochem Biophys 190:514-522
    • (1978) Arch Biochem Biophys , vol.190 , pp. 514-522
    • Yamamoto, H.Y.1    Higashi, R.M.2
  • 53
    • 0015520731 scopus 로고
    • The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region
    • Yamamoto HY, Kamite L (1972) The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region. Biochim Biophys Acta 267:538-543
    • (1972) Biochim Biophys Acta , vol.267 , pp. 538-543
    • Yamamoto, H.Y.1    Kamite, L.2
  • 55
    • 0001504653 scopus 로고
    • An ascorbate-induced absorbance change in chloroplasts from violaxanthin deepoxidation
    • Yamamoto HY, Kamite L, Wang Y-Y (1972) An ascorbate-induced absorbance change in chloroplasts from violaxanthin deepoxidation. Plant Physiol 49:224-228
    • (1972) Plant Physiol , vol.49 , pp. 224-228
    • Yamamoto, H.Y.1    Kamite, L.2    Wang, Y.-Y.3


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