메뉴 건너뛰기




Volumn 89, Issue 2, 2017, Pages 325-337

Functional characterization of UDP-rhamnose-dependent rhamnosyltransferase involved in anthocyanin modification, a key enzyme determining blue coloration in Lobelia erinus

Author keywords

anthocyanin; branch forming GT; Lobelia erinus; lobelinin; modification pathway; rhamnosyltransferase; UDP rhamnose

Indexed keywords

ALUMINUM; CLONING; ENZYMES; FLAVONOIDS; GENES; POLYPEPTIDES; PROTEINS; RECOMBINANT PROTEINS;

EID: 85008469061     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.13387     Document Type: Article
Times cited : (45)

References (54)
  • 2
    • 58149337246 scopus 로고    scopus 로고
    • Structures and antioxidant activity of anthocyanins in many accessions of eggplant and its related species
    • Azuma, K., Ohyama, A., Ippoushi, K., Ichiyanagi, T., Takeuchi, A., Saito, T. and Fukuoka, H. (2008) Structures and antioxidant activity of anthocyanins in many accessions of eggplant and its related species. J. Agric. Food Chem. 56, 10 154–10 159.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10 154-10 159
    • Azuma, K.1    Ohyama, A.2    Ippoushi, K.3    Ichiyanagi, T.4    Takeuchi, A.5    Saito, T.6    Fukuoka, H.7
  • 3
    • 84904815625 scopus 로고    scopus 로고
    • SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information
    • Biasini, M., Bienert, S., Waterhouse, A. et al. (2014) SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252–W258.
    • (2014) Nucleic Acids Res. , vol.42 , pp. W252-W258
    • Biasini, M.1    Bienert, S.2    Waterhouse, A.3
  • 4
    • 38049146159 scopus 로고    scopus 로고
    • Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants
    • Brazier-Hicks, M., Offen, W.A., Gershater, M.C., Revett, T.J., Lim, E., Bowles, D.J., Davies, G.J. and Edwards, R. (2007) Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants. Proc. Natl Acad. Sci. USA, 104, 20 238–202020243.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20 238-202020243
    • Brazier-Hicks, M.1    Offen, W.A.2    Gershater, M.C.3    Revett, T.J.4    Lim, E.5    Bowles, D.J.6    Davies, G.J.7    Edwards, R.8
  • 5
    • 0028133772 scopus 로고
    • Isolation and characterization of a cDNA clone corresponding to the Rt locus of Petunia hybrida
    • Brugliera, F., Holton, T.A., Stevenson, T.W., Farcy, E., Lu, C. and Cornish, E.C. (1994) Isolation and characterization of a cDNA clone corresponding to the Rt locus of Petunia hybrida. Plant J. 5, 81–92.
    • (1994) Plant J. , vol.5 , pp. 81-92
    • Brugliera, F.1    Holton, T.A.2    Stevenson, T.W.3    Farcy, E.4    Lu, C.5    Cornish, E.C.6
  • 6
    • 12144286061 scopus 로고    scopus 로고
    • Changes in the levels of polymethoxyflavones and flavanones as part of the defense mechanism of Citrus sinensis (Cv. Valencia Late) fruits against Phytophthora citrophthora
    • Del Rio, J.A., Gómez, P., Baidez, A.G., Arcas, M.C., Botía, J.M. and Ortuño, A. (2004) Changes in the levels of polymethoxyflavones and flavanones as part of the defense mechanism of Citrus sinensis (Cv. Valencia Late) fruits against Phytophthora citrophthora. J. Agric. Food Chem. 52, 1913–1917.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1913-1917
    • Del Rio, J.A.1    Gómez, P.2    Baidez, A.G.3    Arcas, M.C.4    Botía, J.M.5    Ortuño, A.6
  • 7
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792–1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 8
    • 0000316591 scopus 로고
    • Cloning of the bronze locus in maize by a simple and generalizable procedure using the transposable controlling element Activator (Ac)
    • Fedoroff, N.V., Furtek, D.B. and Jr, O.E.N. (1984) Cloning of the bronze locus in maize by a simple and generalizable procedure using the transposable controlling element Activator (Ac). Proc. Natl Acad. Sci. USA, 81, 3825–3829.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3825-3829
    • Fedoroff, N.V.1    Furtek, D.B.2    Jr, O.E.N.3
  • 9
    • 0032502783 scopus 로고    scopus 로고
    • Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo
    • Ford, C.M., Boss, P.K. and Høj, P.B. (1998) Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273, 9224–9233.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9224-9233
    • Ford, C.M.1    Boss, P.K.2    Høj, P.B.3
  • 10
    • 5144220291 scopus 로고    scopus 로고
    • Citrus fruit bitter flavors: isolation and functional characterization of the gene Cm1,2RhaT encoding a 1,2 rhamnosyltransferase, a key enzyme in the biosynthesis of the bitter flavonoids of citrus
    • Frydman, A., Weisshaus, O., Bar-Peled, M., Huhman, D.V., Sumner, L.W., Marin, F.R., Lewinsohn, E., Fluhr, R., Gressel, J. and Eyal, Y. (2004) Citrus fruit bitter flavors: isolation and functional characterization of the gene Cm1,2RhaT encoding a 1,2 rhamnosyltransferase, a key enzyme in the biosynthesis of the bitter flavonoids of citrus. Plant J. 40, 88–100.
    • (2004) Plant J. , vol.40 , pp. 88-100
    • Frydman, A.1    Weisshaus, O.2    Bar-Peled, M.3    Huhman, D.V.4    Sumner, L.W.5    Marin, F.R.6    Lewinsohn, E.7    Fluhr, R.8    Gressel, J.9    Eyal, Y.10
  • 11
    • 84871957429 scopus 로고    scopus 로고
    • The molecular and enzymatic basis of bitter/non-bitter flavor of citrus fruit: evolution of branch-forming rhamnosyltransferases under domestication
    • Frydman, A., Liberman, R., Huhman, D.V., Carmeli-Weissberg, M., Sapir-Mir, M., Ophir, R., Sumner, L.W. and Eyal, Y. (2013) The molecular and enzymatic basis of bitter/non-bitter flavor of citrus fruit: evolution of branch-forming rhamnosyltransferases under domestication. Plant J. 73, 166–178.
    • (2013) Plant J. , vol.73 , pp. 166-178
    • Frydman, A.1    Liberman, R.2    Huhman, D.V.3    Carmeli-Weissberg, M.4    Sapir-Mir, M.5    Ophir, R.6    Sumner, L.W.7    Eyal, Y.8
  • 12
    • 0038038342 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3’-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from Gentian
    • Fukuchi-Mizutani, M., Okuhara, H., Fukui, Y., Nakao, M., Katsumoto, Y., Yonekura-Sakakibara, K., Kusumi, T., Hase, T. and Tanaka, Y. (2003) Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3’-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from Gentian. Plant Physiol. 132, 1652–1663.
    • (2003) Plant Physiol. , vol.132 , pp. 1652-1663
    • Fukuchi-Mizutani, M.1    Okuhara, H.2    Fukui, Y.3    Nakao, M.4    Katsumoto, Y.5    Yonekura-Sakakibara, K.6    Kusumi, T.7    Hase, T.8    Tanaka, Y.9
  • 14
    • 0036689992 scopus 로고    scopus 로고
    • Changes in flower coloration and sepal anthocyanins of cyanic delphinium cultivars during flowering
    • Hashimoto, F., Tanaka, M., Maeda, H., Fukuda, S., Shimizu, K. and Sakata, Y. (2002) Changes in flower coloration and sepal anthocyanins of cyanic delphinium cultivars during flowering. Biosci. Biotechnol. Biochem. 66, 1652–1659.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1652-1659
    • Hashimoto, F.1    Tanaka, M.2    Maeda, H.3    Fukuda, S.4    Shimizu, K.5    Sakata, Y.6
  • 15
    • 84885574194 scopus 로고    scopus 로고
    • Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea
    • Hiromoto, T., Honjo, E., Tamada, T., Noda, N., Kazuma, K., Suzuki, M. and Kuroki, R. (2013) Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea. J. Synchrotron Rad. 20, 894–898.
    • (2013) J. Synchrotron Rad. , vol.20 , pp. 894-898
    • Hiromoto, T.1    Honjo, E.2    Tamada, T.3    Noda, N.4    Kazuma, K.5    Suzuki, M.6    Kuroki, R.7
  • 16
    • 4644308924 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica
    • Imayama, T., Yoshihara, N., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. (2004) Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167, 1243–1248.
    • (2004) Plant Sci. , vol.167 , pp. 1243-1248
    • Imayama, T.1    Yoshihara, N.2    Fukuchi-Mizutani, M.3    Tanaka, Y.4    Ino, I.5    Yabuya, T.6
  • 17
    • 0242498474 scopus 로고    scopus 로고
    • UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in Arabidopsis thaliana
    • Jones, P., Messner, B., Nakajima, J., Schäffner, A.R. and Saito, K. (2003) UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in Arabidopsis thaliana. J. Biol. Chem. 278, 43 910–43918.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43 910-43918
    • Jones, P.1    Messner, B.2    Nakajima, J.3    Schäffner, A.R.4    Saito, K.5
  • 18
    • 0000205351 scopus 로고
    • Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrid
    • Jonsson, L.M.V., Aarsman, M.E.G., Diepen, J.V., Vlaming, P.D., Smit, N. and Schram, A.W. (1984a) Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrid. Planta, 160, 341–347.
    • (1984) Planta , vol.160 , pp. 341-347
    • Jonsson, L.M.V.1    Aarsman, M.E.G.2    Diepen, J.V.3    Vlaming, P.D.4    Smit, N.5    Schram, A.W.6
  • 19
    • 0000895127 scopus 로고
    • Properties and genetic control of four methyltransferases involved in methylation of anthocyanins in flowers of Petunia hybrid
    • Jonsson, L.M.V., Aarsman, M.E.G., Poulton, J.E. and Schram, A.W. (1984b) Properties and genetic control of four methyltransferases involved in methylation of anthocyanins in flowers of Petunia hybrid. Planta, 160, 174–179.
    • (1984) Planta , vol.160 , pp. 174-179
    • Jonsson, L.M.V.1    Aarsman, M.E.G.2    Poulton, J.E.3    Schram, A.W.4
  • 20
    • 0142187158 scopus 로고    scopus 로고
    • Flavonoid composition related to petal color in different lines of Clitoria ternatea
    • Kazuma, K., Noda, N. and Suzuki, M. (2003) Flavonoid composition related to petal color in different lines of Clitoria ternatea. Phytochemistry, 64, 1133–1139.
    • (2003) Phytochemistry , vol.64 , pp. 1133-1139
    • Kazuma, K.1    Noda, N.2    Suzuki, M.3
  • 21
    • 33749247696 scopus 로고    scopus 로고
    • Identification of delphinidin 3-O-(6′′-O-malonyl)-β-glucoside-3′-O-β-glucoside, a postulated intermediate in the biosynthesis of Ternatin C5 in the blue petals of Clitoria ternatea (Butterfly Pea)
    • Kazuma, K., Kogawa, K., Noda, N., Kato, N. and Suzuki, M. (2004) Identification of delphinidin 3-O-(6′′-O-malonyl)-β-glucoside-3′-O-β-glucoside, a postulated intermediate in the biosynthesis of Ternatin C5 in the blue petals of Clitoria ternatea (Butterfly Pea). Chem. Biodiversity, 1, 1762–1770.
    • (2004) Chem. Biodiversity , vol.1 , pp. 1762-1770
    • Kazuma, K.1    Kogawa, K.2    Noda, N.3    Kato, N.4    Suzuki, M.5
  • 22
    • 35348837144 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase from Clitoria ternatea
    • Kogawa, K., Kato, N., Kazuma, K., Noda, N. and Suzuki, M. (2007) Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase from Clitoria ternatea. Planta, 226, 1501–1509.
    • (2007) Planta , vol.226 , pp. 1501-1509
    • Kogawa, K.1    Kato, N.2    Kazuma, K.3    Noda, N.4    Suzuki, M.5
  • 23
    • 0000569092 scopus 로고
    • Structure of lobelinin A and B, novel anthocyanins acylated with three and four different organic acids, respectively
    • Kondo, T., Yamashiki, J., Kawahori, K. and Goto, T. (1989) Structure of lobelinin A and B, novel anthocyanins acylated with three and four different organic acids, respectively. Tetrahedron Lett. 30, 6055–6058.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 6055-6058
    • Kondo, T.1    Yamashiki, J.2    Kawahori, K.3    Goto, T.4
  • 24
    • 0028082681 scopus 로고
    • Cloning and structural analysis of the anthocyanin pigmentation locus Rt of Petunia hybrida: characterization of insertion sequences in two mutant alleles
    • Kroon, J., Souer, E., Graaff, A.D., Xue, Y., Mol, J. and Koes, R. (1994) Cloning and structural analysis of the anthocyanin pigmentation locus Rt of Petunia hybrida: characterization of insertion sequences in two mutant alleles. Plant J. 5, 69–80.
    • (1994) Plant J. , vol.5 , pp. 69-80
    • Kroon, J.1    Souer, E.2    Graaff, A.D.3    Xue, Y.4    Mol, J.5    Koes, R.6
  • 25
    • 30444443948 scopus 로고    scopus 로고
    • Reciprocal regulation of Arabidopsis UGT78D2 and BANYULS is critical for regulation of the metabolic flux of anthocyanidins to condensed tannins in developing seed coats
    • Lee, Y., Yoon, H.R., Paik, Y.S., Liu, J.R., Chung, W. and Choi, G. (2005) Reciprocal regulation of Arabidopsis UGT78D2 and BANYULS is critical for regulation of the metabolic flux of anthocyanidins to condensed tannins in developing seed coats. J. Plant Biol. 48, 356–370.
    • (2005) J. Plant Biol. , vol.48 , pp. 356-370
    • Lee, Y.1    Yoon, H.R.2    Paik, Y.S.3    Liu, J.R.4    Chung, W.5    Choi, G.6
  • 26
    • 34250172749 scopus 로고    scopus 로고
    • Crystal structure of Medicago truncatula UGT85H2 – insights into the structural basis of a multifunctional (Iso)flavonoid glycosyltransferase
    • Li, L., Modolo, L.V., Escamilla-Trevino, L.L., Achnine, L., Dixon, R.A. and Wang, X. (2007) Crystal structure of Medicago truncatula UGT85H2 – insights into the structural basis of a multifunctional (Iso)flavonoid glycosyltransferase. J. Mol. Biol. 370, 951–963.
    • (2007) J. Mol. Biol. , vol.370 , pp. 951-963
    • Li, L.1    Modolo, L.V.2    Escamilla-Trevino, L.L.3    Achnine, L.4    Dixon, R.A.5    Wang, X.6
  • 27
    • 78650621959 scopus 로고    scopus 로고
    • Identification and characterisation of F3GT1 and F3GGT1, two glycosyltransferases responsible for anthocyanin biosynthesis in red-fleshed kiwifruit (Actinidia chinensis)
    • Montefiori, M., Espley, R.V., Stevenson, D., Cooney, J., Datson, P.M., Saiz, A., Atkinson, R.G., Hellens, R.P. and Allan, A.C. (2011) Identification and characterisation of F3GT1 and F3GGT1, two glycosyltransferases responsible for anthocyanin biosynthesis in red-fleshed kiwifruit (Actinidia chinensis). Plant J. 65, 106–118.
    • (2011) Plant J. , vol.65 , pp. 106-118
    • Montefiori, M.1    Espley, R.V.2    Stevenson, D.3    Cooney, J.4    Datson, P.M.5    Saiz, A.6    Atkinson, R.G.7    Hellens, R.P.8    Allan, A.C.9
  • 28
    • 21044437332 scopus 로고    scopus 로고
    • Japanese morning glory dusky mutants displaying reddish-brown or purplish-gray flowers are deficient in a novel glycosylation enzyme for anthocyanin biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2′′-O-glucosyltransferase, due to 4-bp insertions in the gene
    • Morita, Y., Hoshino, A., Kikuchi, Y. et al. (2005) Japanese morning glory dusky mutants displaying reddish-brown or purplish-gray flowers are deficient in a novel glycosylation enzyme for anthocyanin biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2′′-O-glucosyltransferase, due to 4-bp insertions in the gene. Plant J. 42, 353–363.
    • (2005) Plant J. , vol.42 , pp. 353-363
    • Morita, Y.1    Hoshino, A.2    Kikuchi, Y.3
  • 29
    • 0035854832 scopus 로고    scopus 로고
    • Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis
    • Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. (2001) Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276, 25 797–25 803.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25 797-25 803
    • Nakajima, J.1    Tanaka, Y.2    Yamazaki, M.3    Saito, K.4
  • 30
    • 45549106858 scopus 로고    scopus 로고
    • Cloning and characterization of the UDP-glucose:anthocyanin 5-O-glucosyltransferase gene from blue-flowered gentian
    • Nakatsuka, T., Sato, K., Takahashi, H., Yamamura, S. and Nishihara, M. (2008) Cloning and characterization of the UDP-glucose:anthocyanin 5-O-glucosyltransferase gene from blue-flowered gentian. J. Exp. Bot. 59, 1241–1252.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1241-1252
    • Nakatsuka, T.1    Sato, K.2    Takahashi, H.3    Yamamura, S.4    Nishihara, M.5
  • 31
    • 84855648685 scopus 로고    scopus 로고
    • Structure of the acyl-glucose-dependent anthocyanin 5-O-glucosyltransferase gene in carnations and its disruption by transposable elements in some varieties
    • Nishizaki, Y., Matsuba, Y., Okamoto, E., Okamura, M., Ozeki, Y. and Sasaki, N. (2011) Structure of the acyl-glucose-dependent anthocyanin 5-O-glucosyltransferase gene in carnations and its disruption by transposable elements in some varieties. Mol. Genet. Genomics 286, 383–394.
    • (2011) Mol. Genet. Genomics , vol.286 , pp. 383-394
    • Nishizaki, Y.1    Matsuba, Y.2    Okamoto, E.3    Okamura, M.4    Ozeki, Y.5    Sasaki, N.6
  • 34
    • 77957182240 scopus 로고
    • Construction and expression in tobacco of a β-glucuronidase (GUS) reporter gene containing an intron within the coding sequence
    • Ohta, S., Mita, S., Hattori, T. and Nakamura, K. (1990) Construction and expression in tobacco of a β-glucuronidase (GUS) reporter gene containing an intron within the coding sequence. Plant Cell Physiol. 31, 805–813.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 805-813
    • Ohta, S.1    Mita, S.2    Hattori, T.3    Nakamura, K.4
  • 35
    • 34247099779 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-d-glucose to UDP-l-rhamnose conversion
    • Oka, T., Nemoto, T. and Jigami, Y. (2007) Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-d-glucose to UDP-l-rhamnose conversion. J. Biol. Chem. 282, 5389–5403.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5389-5403
    • Oka, T.1    Nemoto, T.2    Jigami, Y.3
  • 36
    • 84890877625 scopus 로고    scopus 로고
    • Linkage mapping, molecular cloning and functional analysis of soybean gene Fg2 encoding flavonol 3-O-glucoside (1 → 6) Rhamnosyltransferase
    • Rodas, F.R., Rodriguez, T.O., Murai, Y. et al. (2014) Linkage mapping, molecular cloning and functional analysis of soybean gene Fg2 encoding flavonol 3-O-glucoside (1 → 6) Rhamnosyltransferase. Plant Mol. Biol. 84, 287–300.
    • (2014) Plant Mol. Biol. , vol.84 , pp. 287-300
    • Rodas, F.R.1    Rodriguez, T.O.2    Murai, Y.3
  • 38
    • 12544253335 scopus 로고    scopus 로고
    • UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers: enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis
    • Sawada, S., Suzuki, H., Ichimaida, F., Yamaguchi, M., Iwashita, T., Fukui, Y., Hemmi, H., Nishino, T. and Nakayama, T. (2005) UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers: enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis. J. Biol. Chem. 280, 899–906.
    • (2005) J. Biol. Chem. , vol.280 , pp. 899-906
    • Sawada, S.1    Suzuki, H.2    Ichimaida, F.3    Yamaguchi, M.4    Iwashita, T.5    Fukui, Y.6    Hemmi, H.7    Nishino, T.8    Nakayama, T.9
  • 39
    • 33645281589 scopus 로고    scopus 로고
    • Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula
    • Shao, H., He, X., Achnine, L., Blount, J.W., Dixon, R.A. and Wang, X. (2005) Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula. Plant Cell, 17, 3141–3154.
    • (2005) Plant Cell , vol.17 , pp. 3141-3154
    • Shao, H.1    He, X.2    Achnine, L.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 40
    • 77952953046 scopus 로고    scopus 로고
    • Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max
    • Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. (2010) Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584, 2258–2264.
    • (2010) FEBS Lett. , vol.584 , pp. 2258-2264
    • Shibuya, M.1    Nishimura, K.2    Yasuyama, N.3    Ebizuka, Y.4
  • 41
    • 15744404020 scopus 로고    scopus 로고
    • Effects of UV-B radiation, cold and desiccation stress on rutin concentration and rutin glucosidase activity in tartary buckwheat (Fagopyrum tataricum) leaves
    • Suzuki, T., Honda, Y. and Mukasa, Y. (2005) Effects of UV-B radiation, cold and desiccation stress on rutin concentration and rutin glucosidase activity in tartary buckwheat (Fagopyrum tataricum) leaves. Plant Sci. 168, 1303–1307.
    • (2005) Plant Sci. , vol.168 , pp. 1303-1307
    • Suzuki, T.1    Honda, Y.2    Mukasa, Y.3
  • 43
    • 43549088323 scopus 로고    scopus 로고
    • Biosynthesis of plant pigments: anthocyanins, betalains and carotenoids
    • Tanaka, Y., Sasaki, N. and Ohmiya, A. (2008) Biosynthesis of plant pigments: anthocyanins, betalains and carotenoids. Plant J. 54, 733–749.
    • (2008) Plant J. , vol.54 , pp. 733-749
    • Tanaka, Y.1    Sasaki, N.2    Ohmiya, A.3
  • 44
    • 84955272130 scopus 로고    scopus 로고
    • Flower colors and their anthocyanins in Saintpaulia cultivars (Gesneriaceae)
    • Tatsuzawa, F. and Hosokawa, M. (2015) Flower colors and their anthocyanins in Saintpaulia cultivars (Gesneriaceae). Hort. J. 85, 63–69.
    • (2015) Hort. J. , vol.85 , pp. 63-69
    • Tatsuzawa, F.1    Hosokawa, M.2
  • 45
    • 2442620501 scopus 로고    scopus 로고
    • High-frequency transformation of Lobelia erinus L. by Agrobacterium-mediated gene transfer
    • Tsugawa, H., Kagami, T. and Suzuki, M. (2004) High-frequency transformation of Lobelia erinus L. by Agrobacterium-mediated gene transfer. Plant Cell Rep. 22, 759–764.
    • (2004) Plant Cell Rep. , vol.22 , pp. 759-764
    • Tsugawa, H.1    Kagami, T.2    Suzuki, M.3
  • 46
    • 0025386677 scopus 로고
    • Nucleotide sequence of the Bronze-1 homologous gene from Hordeum vulgare
    • Wise, R.P., Rohde, W. and Salamini, F. (1990) Nucleotide sequence of the Bronze-1 homologous gene from Hordeum vulgare. Plant Mol. Biol. 14, 277–279.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 277-279
    • Wise, R.P.1    Rohde, W.2    Salamini, F.3
  • 47
    • 0036100332 scopus 로고    scopus 로고
    • Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata
    • Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino, I. (2002) Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162, 779–784.
    • (2002) Plant Sci. , vol.162 , pp. 779-784
    • Yabuya, T.1    Yamaguchi, M.2    Imayama, T.3    Katoh, K.4    Ino, I.5
  • 48
    • 0033548604 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin
    • Yamazaki, M., Gong, Z., Fukuchi-Mizutani, M., Fukui, Y., Tanaka, Y., Kusumi, T. and Saito, K. (1999) Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin. J. Biol. Chem. 274, 7405–7411.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7405-7411
    • Yamazaki, M.1    Gong, Z.2    Fukuchi-Mizutani, M.3    Fukui, Y.4    Tanaka, Y.5    Kusumi, T.6    Saito, K.7
  • 49
    • 0036009060 scopus 로고    scopus 로고
    • Two flavonoid glucosyltransferases from Petunia hybrida: molecular cloning, biochemical properties and developmentally regulated expression
    • Yamazaki, M., Yamagishi, E., Gong, Z., Fukuchi-Mizutani, M., Fukui, Y., Tanaka, Y., Kusumi, T., Yamaguchi, M. and Saito, K. (2002) Two flavonoid glucosyltransferases from Petunia hybrida: molecular cloning, biochemical properties and developmentally regulated expression. Plant Mol. Biol. 48, 401–411.
    • (2002) Plant Mol. Biol. , vol.48 , pp. 401-411
    • Yamazaki, M.1    Yamagishi, E.2    Gong, Z.3    Fukuchi-Mizutani, M.4    Fukui, Y.5    Tanaka, Y.6    Kusumi, T.7    Yamaguchi, M.8    Saito, K.9
  • 50
    • 34447502537 scopus 로고    scopus 로고
    • Identification of a flavonol 7-O-rhamnosyltransferase gene determining flavonoid pattern in Arabidopsis by transcriptome coexpression analysis and reverse genetics
    • Yonekura-Sakakibara, K., Tohge, T., Niida, R. and Saito, K. (2007) Identification of a flavonol 7-O-rhamnosyltransferase gene determining flavonoid pattern in Arabidopsis by transcriptome coexpression analysis and reverse genetics. J. Biol. Chem. 282, 14 932–14 941.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14 932-14 941
    • Yonekura-Sakakibara, K.1    Tohge, T.2    Niida, R.3    Saito, K.4
  • 51
    • 84355166610 scopus 로고    scopus 로고
    • Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana
    • Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R. et al. (2012) Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69, 154–167.
    • (2012) Plant J. , vol.69 , pp. 154-167
    • Yonekura-Sakakibara, K.1    Fukushima, A.2    Nakabayashi, R.3
  • 52
    • 0034037565 scopus 로고    scopus 로고
    • Contribution of each caffeoyl residue of the pigment molecule of gentiodelphin to blue color development
    • Yoshida, K., Toyama, Y., Kameda, K. and Kondo, T. (2000) Contribution of each caffeoyl residue of the pigment molecule of gentiodelphin to blue color development. Phytochemistry, 54, 85–92.
    • (2000) Phytochemistry , vol.54 , pp. 85-92
    • Yoshida, K.1    Toyama, Y.2    Kameda, K.3    Kondo, T.4
  • 53
    • 69549142942 scopus 로고    scopus 로고
    • Blue flower color development by anthocyanins: from chemical structure to cell physiology
    • Yoshida, K., Mori, M. and Kondo, T. (2009) Blue flower color development by anthocyanins: from chemical structure to cell physiology. Nat. Prod. Rep. 26, 884–915.
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 884-915
    • Yoshida, K.1    Mori, M.2    Kondo, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.