메뉴 건너뛰기




Volumn 69, Issue 6, 2012, Pages 1030-1042

A genome-wide phylogenetic reconstruction of family 1 UDP- glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land

Author keywords

A. thaliana; glycosyltransferases; molecular evolution; phylogenetic analysis; plant genome; PSPG motif

Indexed keywords

GLYCOSYLTRANSFERASES; MOLECULAR EVOLUTION; PHYLOGENETIC ANALYSIS; PLANT GENOMES; PSPG MOTIF; THALIANA;

EID: 84859165041     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2011.04853.x     Document Type: Article
Times cited : (269)

References (73)
  • 1
    • 79956309501 scopus 로고    scopus 로고
    • The Selaginella genome identifies genetic changes associated with the evolution of vascular plants
    • Banks, J.A., Nishiyama, T., Hasebe, M., et al. (2011) The Selaginella genome identifies genetic changes associated with the evolution of vascular plants. Science, 332, 960-963.
    • (2011) Science , vol.332 , pp. 960-963
    • Banks, J.A.1    Nishiyama, T.2    Hasebe, M.3
  • 4
    • 34547567501 scopus 로고    scopus 로고
    • Selection of plants for roles in phytoremediation: The importance of glucosylation
    • Brazier-Hicks, M., Edwards, L.A., and, Edwards, R., (2007a) Selection of plants for roles in phytoremediation: the importance of glucosylation. Plant Biotechnol. J. 5, 627-635.
    • (2007) Plant Biotechnol. J. , vol.5 , pp. 627-635
    • Brazier-Hicks, M.1    Edwards, L.A.2    Edwards, R.3
  • 6
    • 53849136229 scopus 로고    scopus 로고
    • Discovery of new biocatalysts for the glycosylation of terpenoid scaffolds
    • Caputi, L., Lim, E.K., and, Bowles, D.J., (2008) Discovery of new biocatalysts for the glycosylation of terpenoid scaffolds. Chemistry, 14, 6656-6662.
    • (2008) Chemistry , vol.14 , pp. 6656-6662
    • Caputi, L.1    Lim, E.K.2    Bowles, D.J.3
  • 7
    • 80052346740 scopus 로고    scopus 로고
    • Establishing a time-scale for plant evolution
    • Clarke, J.T., Warnock, R.C., and, Donoghue, P.C., (2011) Establishing a time-scale for plant evolution. New Phytol. 192, 266-301.
    • (2011) New Phytol. , vol.192 , pp. 266-301
    • Clarke, J.T.1    Warnock, R.C.2    Donoghue, P.C.3
  • 8
    • 0346306092 scopus 로고    scopus 로고
    • Why are there so many carbohydrate-active enzyme-related genes in plants?
    • Coutinho, P.M., Stam, M., Blanc, E., and, Henrissat, B., (2003) Why are there so many carbohydrate-active enzyme-related genes in plants? Trends Plant Sci. 8, 563-565.
    • (2003) Trends Plant Sci. , vol.8 , pp. 563-565
    • Coutinho, P.M.1    Stam, M.2    Blanc, E.3    Henrissat, B.4
  • 10
    • 70349202978 scopus 로고    scopus 로고
    • Mutations in UDP-Glucose:sterol glucosyltransferase in Arabidopsis cause transparent testa phenotype and suberization defect in seeds
    • DeBolt, S., Scheible, W.R., Schrick, K., et al. (2009) Mutations in UDP-Glucose:sterol glucosyltransferase in Arabidopsis cause transparent testa phenotype and suberization defect in seeds. Plant Physiol. 151, 78-87.
    • (2009) Plant Physiol. , vol.151 , pp. 78-87
    • Debolt, S.1    Scheible, W.R.2    Schrick, K.3
  • 11
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment method with reduced time and space complexity
    • Edgar, R.C., (2004) MUSCLE: multiple sequence alignment method with reduced time and space complexity. Nucleic Acids Res. 32, 1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 12
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson, O., Brunak, S., von Heijne, G., and, Nielsen, H., (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protoc. 2, 953-971.
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 13
    • 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 glycosylate anthocyanidins in vivo
    • Ford, C.M., Boss, P.K., and, Hoj, 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 glycosylate 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    Hoj, P.B.3
  • 14
    • 27644476269 scopus 로고    scopus 로고
    • Plant secondary metabolism glycosyltransferases: The emerging functional analysis
    • Gachon, C.M., Langlois-Meurinne, M., and, Saindrenan, P., (2005) Plant secondary metabolism glycosyltransferases: the emerging functional analysis. Trends Plant Sci. 10, 542-549.
    • (2005) Trends Plant Sci. , vol.10 , pp. 542-549
    • Gachon, C.M.1    Langlois-Meurinne, M.2    Saindrenan, P.3
  • 15
    • 57549102935 scopus 로고    scopus 로고
    • Detoxification of the explosive 2,4,6-trinitrotoluene in A. thaliana: Discovery of bifunctional O- and C-glucosyltransferases
    • Gandia-Herrero, F., Lorenz, A., Larson, T., Graham, I.A., Bowles, D.J., Rylott, E.L., and, Bruce, N.C., (2008) Detoxification of the explosive 2,4,6-trinitrotoluene in A. thaliana: discovery of bifunctional O- and C-glucosyltransferases. Plant J. 56, 963-974.
    • (2008) Plant J. , vol.56 , pp. 963-974
    • Gandia-Herrero, F.1    Lorenz, A.2    Larson, T.3    Graham, I.A.4    Bowles, D.J.5    Rylott, E.L.6    Bruce, N.C.7
  • 16
    • 77349113758 scopus 로고    scopus 로고
    • Cloning and heterologous expression of glycosyltransferases from Malus × domestica and Pyrus communis, which convertphloretin to phloretin 2′-O-glucoside (phloridzin)
    • Gosch, C., Halbwirth, H., Schneider, B., Hölscher, D., and, Stich, K., (2010) Cloning and heterologous expression of glycosyltransferases from Malus × domestica and Pyrus communis, which convertphloretin to phloretin 2′-O-glucoside (phloridzin). Plant Sci. 178, 299-306.
    • (2010) Plant Sci. , vol.178 , pp. 299-306
    • Gosch, C.1    Halbwirth, H.2    Schneider, B.3    Hölscher, D.4    Stich, K.5
  • 17
    • 33846898073 scopus 로고    scopus 로고
    • Mesocarp localization of a bifunctional resveratrol/hydrocinnamic acid glucosyltransferase of Concord grape (Vitis labrusca)
    • Hall, D., and, De Luca, V., (2007) Mesocarp localization of a bifunctional resveratrol/hydrocinnamic acid glucosyltransferase of Concord grape (Vitis labrusca). Plant J. 49, 579-591.
    • (2007) Plant J. , vol.49 , pp. 579-591
    • Hall, D.1    De Luca, V.2
  • 18
    • 0042322325 scopus 로고    scopus 로고
    • The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor
    • Hansen, K.S., Kristensen, C., Tattersall, D.B., Jones, P.R., Olsen, C.E., Bak, S., and, Møller, B.L., (2003) The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor. Phytochemistry, 64, 143-151.
    • (2003) Phytochemistry , vol.64 , pp. 143-151
    • Hansen, K.S.1    Kristensen, C.2    Tattersall, D.B.3    Jones, P.R.4    Olsen, C.E.5    Bak, S.6    Møller, B.L.7
  • 19
    • 9144241791 scopus 로고    scopus 로고
    • N-glucosylation of cytokinins by glycosyltransferases from A. thaliana
    • Hou, B., Lim, E.K., Higgins, G.S., and, Bowles, D.J., (2004) N-glucosylation of cytokinins by glycosyltransferases from A. thaliana. J. Biol. Chem. 279, 47822-47832.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47822-47832
    • Hou, B.1    Lim, E.K.2    Higgins, G.S.3    Bowles, D.J.4
  • 20
    • 70649085835 scopus 로고    scopus 로고
    • The genome of the cucumber, Cucumis sativus L
    • Huang, S., Li, R., Zhang, Z., et al. (2009) The genome of the cucumber, Cucumis sativus L. Nat. Genet. 41, 1275-1281.
    • (2009) Nat. Genet. , vol.41 , pp. 1275-1281
    • Huang, S.1    Li, R.2    Zhang, Z.3
  • 21
    • 79953113773 scopus 로고    scopus 로고
    • Overexpression of the UGT73C6 alters brassinosteroid glucoside formation in Arabidopsis thaliana
    • Husar, S., Berthiller, F., Fujioka, S., et al. (2011) Overexpression of the UGT73C6 alters brassinosteroid glucoside formation in Arabidopsis thaliana. BMC Plant Biol. 11, 51.
    • (2011) BMC Plant Biol. , vol.11 , pp. 51
    • Husar, S.1    Berthiller, F.2    Fujioka, S.3
  • 23
    • 0035830910 scopus 로고    scopus 로고
    • Identification and biochemical characterization of an A. thaliana indole-3-acetic acid glucosyltransferase
    • Jackson, R.G., Lim, E.K., Li, Y., Kowalczyk, M., Sandberg, G., Hoggett, J., Ashford, D.A., and, Bowles, D.J., (2001) Identification and biochemical characterization of an A. thaliana indole-3-acetic acid glucosyltransferase. J. Biol. Chem. 276, 4350-4356.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4350-4356
    • Jackson, R.G.1    Lim, E.K.2    Li, Y.3    Kowalczyk, M.4    Sandberg, G.5    Hoggett, J.6    Ashford, D.A.7    Bowles, D.J.8
  • 24
    • 0013254684 scopus 로고    scopus 로고
    • Over-expression of an A. thaliana gene encoding a glucosyltransferase of indole-3-acetic acid: Phenotypic characterization of transgenic lines
    • Jackson, R.G., Kowalczyk, M., Li, Y., Higgins, G., Ross, J., Sandberg, G., and, Bowles, D.J., (2002) Over-expression of an A. thaliana gene encoding a glucosyltransferase of indole-3-acetic acid: phenotypic characterization of transgenic lines. Plant J. 32, 573-583.
    • (2002) Plant J. , vol.32 , pp. 573-583
    • Jackson, R.G.1    Kowalczyk, M.2    Li, Y.3    Higgins, G.4    Ross, J.5    Sandberg, G.6    Bowles, D.J.7
  • 25
    • 34848886909 scopus 로고    scopus 로고
    • The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla
    • Jaillon, O., Aury, J.M., Noel, B., et al. (2007) The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla. Nature, 449, 463-467.
    • (2007) Nature , vol.449 , pp. 463-467
    • Jaillon, O.1    Aury, J.M.2    Noel, B.3
  • 26
    • 0033544872 scopus 로고    scopus 로고
    • The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate activity
    • Jones, P.R., Møller, B.L., and, Hoj, P.B., (1999) The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate activity. J. Biol. Chem. 274, 35483-35491.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35483-35491
    • Jones, P.R.1    Møller, B.L.2    Hoj, P.B.3
  • 27
    • 0242498474 scopus 로고    scopus 로고
    • UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in A. thaliana thaliana
    • Jones, P., Messner, B., Nakajima, J., Schäffner, A.R., and, Saito, K., (2003) UGT73C6 and UGT78D1, glycosyltransferases involved in flavonol glycoside biosynthesis in A. thaliana thaliana. J. Biol. Chem. 278, 43910-43918.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43910-43918
    • Jones, P.1    Messner, B.2    Nakajima, J.3    Schäffner, A.R.4    Saito, K.5
  • 28
    • 47249147654 scopus 로고    scopus 로고
    • Isolation and characterization of a novel glycosyltransferase that converts phloretin to phlorizin, a potent antioxidant in apple
    • Jugdé, H., Nguy, D., Moller, I., Cooney, J.M., and, Atkinson, R.G., (2008) Isolation and characterization of a novel glycosyltransferase that converts phloretin to phlorizin, a potent antioxidant in apple. FEBS J. 275, 3804-3814.
    • (2008) FEBS J. , vol.275 , pp. 3804-3814
    • Jugdé, H.1    Nguy, D.2    Moller, I.3    Cooney, J.M.4    Atkinson, R.G.5
  • 29
    • 77954242456 scopus 로고    scopus 로고
    • Functional characterization of a UDP-glucose:flavonoid 3-O-glucosyltransferase from the seed coat of black soybean (Glycine max (L.) Merr.)
    • Kovinich, N., Saleem, A., Arnason, J.T., and, Miki, B., (2010) Functional characterization of a UDP-glucose:flavonoid 3-O-glucosyltransferase from the seed coat of black soybean (Glycine max (L.) Merr.). Phytochemistry, 71, 1253-1263.
    • (2010) Phytochemistry , vol.71 , pp. 1253-1263
    • Kovinich, N.1    Saleem, A.2    Arnason, J.T.3    Miki, B.4
  • 30
    • 4143092938 scopus 로고    scopus 로고
    • Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation
    • Kubo, A., Arai, Y., Nagashima, S., and, Yoshikawa, T., (2004) Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation. Arch. Biochem. Biophys. 429, 198-203.
    • (2004) Arch. Biochem. Biophys. , vol.429 , pp. 198-203
    • Kubo, A.1    Arai, Y.2    Nagashima, S.3    Yoshikawa, T.4
  • 31
    • 33749242053 scopus 로고    scopus 로고
    • The glucosyltransferase UGT72E2 is responsible for monolignol 4-O-glucoside production in A. thaliana thaliana
    • Lanot, A., Hodge, D., Jackson, R.G., George, G.L., Elias, L., Lim, E.K., Vaistij, F.E., and, Bowles, D.J., (2006) The glucosyltransferase UGT72E2 is responsible for monolignol 4-O-glucoside production in A. thaliana thaliana. Plant J. 48, 286-295.
    • (2006) Plant J. , vol.48 , pp. 286-295
    • Lanot, A.1    Hodge, D.2    Jackson, R.G.3    George, G.L.4    Elias, L.5    Lim, E.K.6    Vaistij, F.E.7    Bowles, D.J.8
  • 32
    • 0035830930 scopus 로고    scopus 로고
    • Phylogenetic analysis of the UDP-glycosyltransferase multigene family of A. thaliana thaliana
    • Li, Y., Baldauf, S., Lim, E.K., and, Bowles, D.J., (2001) Phylogenetic analysis of the UDP-glycosyltransferase multigene family of A. thaliana thaliana. J. Biol. Chem. 276, 4338-4343.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4338-4343
    • Li, Y.1    Baldauf, S.2    Lim, E.K.3    Bowles, D.J.4
  • 33
    • 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
  • 34
    • 0037016740 scopus 로고    scopus 로고
    • The activity of A. thaliana glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates
    • Lim, E.K., Doucet, C.J., Li, Y., Elias, L., Worrall, D., Spencer, S.P., Ross, J., and, Bowles, D.J., (2002) The activity of A. thaliana glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates. J. Biol. Chem. 277, 586-592.
    • (2002) J. Biol. Chem. , vol.277 , pp. 586-592
    • Lim, E.K.1    Doucet, C.J.2    Li, Y.3    Elias, L.4    Worrall, D.5    Spencer, S.P.6    Ross, J.7    Bowles, D.J.8
  • 36
    • 0043069756 scopus 로고    scopus 로고
    • Regioselectivity of glucosylation of caffeic acid by a UDP-glucose:glucosyltransferase is maintained in planta
    • Lim, E.K., Higgins, G.S., and, Bowles, D.J., (2003b) Regioselectivity of glucosylation of caffeic acid by a UDP-glucose:glucosyltransferase is maintained in planta. Biochem. J. 373, 987-992.
    • (2003) Biochem. J. , vol.373 , pp. 987-992
    • Lim, E.K.1    Higgins, G.S.2    Bowles, D.J.3
  • 37
    • 4143140277 scopus 로고    scopus 로고
    • A. thaliana glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides
    • Lim, E.K., Ashford, D.A., Hou, B., Jackson, R.G., and, Bowles, D.J., (2004) A. thaliana glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides. Biotechnol. Bioeng. 87, 623-631.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 623-631
    • Lim, E.K.1    Ashford, D.A.2    Hou, B.3    Jackson, R.G.4    Bowles, D.J.5
  • 38
    • 68249122636 scopus 로고    scopus 로고
    • Engineering Flax with the GT Family 1 Solanum sogarandium Glycosyltransferase SsGT1 confers increased resistance to Fusarium infection
    • Lorenc-Kukula, K., Zuk, M., Kulma, A., Czemplik, M., Kostyn, K., Skala, J., Starzycki, M., and, Szopa, J., (2009) Engineering Flax with the GT Family 1 Solanum sogarandium Glycosyltransferase SsGT1 confers increased resistance to Fusarium infection. J. Agric. Food. Chem. 57, 6698-6705.
    • (2009) J. Agric. Food. Chem. , vol.57 , pp. 6698-6705
    • Lorenc-Kukula, K.1    Zuk, M.2    Kulma, A.3    Czemplik, M.4    Kostyn, K.5    Skala, J.6    Starzycki, M.7    Szopa, J.8
  • 39
    • 0033150352 scopus 로고    scopus 로고
    • A gene encoding the cytokinin enzyme zeatin O-xylosyltransferase of Phaseolus vulgaris
    • Martin, R.C., Mok, M.C., and, Mok, D.W., (1999) A gene encoding the cytokinin enzyme zeatin O-xylosyltransferase of Phaseolus vulgaris. Plant Physiol. 120, 553-558.
    • (1999) Plant Physiol. , vol.120 , pp. 553-558
    • Martin, R.C.1    Mok, M.C.2    Mok, D.W.3
  • 40
    • 0035826722 scopus 로고    scopus 로고
    • A maize cytokinin gene encoding an O-glucosyltransferase specific to cis-zeatin
    • Martin, R.C., Mok, M.C., Habben, J.E., and, Mok, D.W., (2001) A maize cytokinin gene encoding an O-glucosyltransferase specific to cis-zeatin. Proc. Natl. Acad. Sci. USA, 98, 5922-5926.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5922-5926
    • Martin, R.C.1    Mok, M.C.2    Habben, J.E.3    Mok, D.W.4
  • 41
    • 34249709591 scopus 로고    scopus 로고
    • A single amino acid in the PSPG-box plays an important role in the catalytic function of CaUGT2 (Curcumin glucosyltransferase), a group d family 1 glucosyltransferase from Catharanthus roseus
    • Masada, S., Terasaka, K., and, Mizukami, H., (2007) A single amino acid in the PSPG-box plays an important role in the catalytic function of CaUGT2 (Curcumin glucosyltransferase), a group d family 1 glucosyltransferase from Catharanthus roseus. FEBS Lett. 581, 2605-2610.
    • (2007) FEBS Lett. , vol.581 , pp. 2605-2610
    • Masada, S.1    Terasaka, K.2    Mizukami, H.3
  • 42
    • 0033607802 scopus 로고    scopus 로고
    • Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida
    • Miller, K.D., Guyon, V., Evans, J.N., Shuttleworth, W.A., and, Taylor, L.P., (1999) Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida. J. Biol. Chem. 274, 34011-34019.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34011-34019
    • Miller, K.D.1    Guyon, V.2    Evans, J.N.3    Shuttleworth, W.A.4    Taylor, L.P.5
  • 43
    • 34250179856 scopus 로고    scopus 로고
    • A functional genomics approach to (iso)flavonoid glycosylation in the model legume Medicago truncatula
    • Modolo, L.V., Blount, J.W., Achnine, L., Naoumkina, M.A., Wang, X., and, Dixon, R.A., (2007) A functional genomics approach to (iso)flavonoid glycosylation in the model legume Medicago truncatula. Plant Mol. Biol. 64, 499-518.
    • (2007) Plant Mol. Biol. , vol.64 , pp. 499-518
    • Modolo, L.V.1    Blount, J.W.2    Achnine, L.3    Naoumkina, M.A.4    Wang, X.5    Dixon, R.A.6
  • 44
    • 7044231921 scopus 로고    scopus 로고
    • Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas
    • Moraga, A.R., Nohales, P.F., Perez, J.A., and, Gomez-Gomez, L., (2004) Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta, 219, 955-966.
    • (2004) Planta , vol.219 , pp. 955-966
    • Moraga, A.R.1    Nohales, P.F.2    Perez, J.A.3    Gomez-Gomez, L.4
  • 45
    • 34548155465 scopus 로고    scopus 로고
    • A UDP-glucose:isoflavone 7-O-glucosyltransferase from the roots of soybean (Glycine max) seedlings. Purification, gene cloning, phylogenetics, and an implication for an alternative strategy of enzyme catalysis
    • Noguchi, A., Saito, A., Homma, Y., Nakao, M., Sasaki, N., Nischino, T., Takahashi, S., and, Nakayama, T., (2007) A UDP-glucose:isoflavone 7-O-glucosyltransferase from the roots of soybean (Glycine max) seedlings. Purification, gene cloning, phylogenetics, and an implication for an alternative strategy of enzyme catalysis. J. Biol. Chem. 282, 23581-23590.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23581-23590
    • Noguchi, A.1    Saito, A.2    Homma, Y.3    Nakao, M.4    Sasaki, N.5    Nischino, T.6    Takahashi, S.7    Nakayama, T.8
  • 47
    • 77957806566 scopus 로고    scopus 로고
    • Functional differentiation of the glycosyltransferases that contribute to the chemical diversity of bioactive flavonol glycosides in grapevines (Vitis vinifera)
    • Ono, E., Homma, Y., Horikawa, M., Kunikane-Doi, S., Imai, H., Takahashi, S., Kawai, Y., Ishiguro, M., Fukui, Y., and, Nakayama, T., (2010) Functional differentiation of the glycosyltransferases that contribute to the chemical diversity of bioactive flavonol glycosides in grapevines (Vitis vinifera). Plant Cell, 22, 2856-2871.
    • (2010) Plant Cell , vol.22 , pp. 2856-2871
    • Ono, E.1    Homma, Y.2    Horikawa, M.3    Kunikane-Doi, S.4    Imai, H.5    Takahashi, S.6    Kawai, Y.7    Ishiguro, M.8    Fukui, Y.9    Nakayama, T.10
  • 48
    • 57749111577 scopus 로고    scopus 로고
    • Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: Molecular modeling substantiated by site-specific mutagenesis and biochemical analyses
    • Osmani, S.A., Bak, S., Imberty, A., Olsen, C.E., and, Møller, B.L., (2008) Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses. Plant Physiol. 48, 1295-1308.
    • (2008) Plant Physiol. , vol.48 , pp. 1295-1308
    • Osmani, S.A.1    Bak, S.2    Imberty, A.3    Olsen, C.E.4    Møller, B.L.5
  • 49
    • 62349122684 scopus 로고    scopus 로고
    • Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling
    • Osmani, S.A., Bak, S., and, Møller, B.L., (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry, 70, 325-347.
    • (2009) Phytochemistry , vol.70 , pp. 325-347
    • Osmani, S.A.1    Bak, S.2    Møller, B.L.3
  • 50
    • 0037067755 scopus 로고    scopus 로고
    • The donor substrate specificity of the human β1,3- glucuronosyltransferase i (GlcAT-I) towards UDP-glucuronic acid is determined by two crucial histidine and arginine residues
    • Ouzzine, M., Gulberti, S., Netter, P., Magdalou, J., and, Fournel-Gigleux, S., (2002) The donor substrate specificity of the human β1,3-glucuronosyltransferase I (GlcAT-I) towards UDP-glucuronic acid is determined by two crucial histidine and arginine residues. J. Biol. Chem. 277, 25439-25445.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25439-25445
    • Ouzzine, M.1    Gulberti, S.2    Netter, P.3    Magdalou, J.4    Fournel-Gigleux, S.5
  • 51
    • 0037309606 scopus 로고    scopus 로고
    • On the origin of family 1 plant glycosyltransferases
    • Paquette, S., Møller, B.L., and, Bak, S., (2003) On the origin of family 1 plant glycosyltransferases. Phytochemistry, 62, 399-413.
    • (2003) Phytochemistry , vol.62 , pp. 399-413
    • Paquette, S.1    Møller, B.L.2    Bak, S.3
  • 52
    • 58449137410 scopus 로고    scopus 로고
    • The Sorghum bicolor genome and the diversification of grasses
    • Paterson, A.H., Bowers, J.E., Bruggmann, R., et al. (2009) The Sorghum bicolor genome and the diversification of grasses. Nature, 457, 551-556.
    • (2009) Nature , vol.457 , pp. 551-556
    • Paterson, A.H.1    Bowers, J.E.2    Bruggmann, R.3
  • 53
    • 79959371658 scopus 로고    scopus 로고
    • Plant biology. Green genomes
    • Pennisi, E., (2011) Plant biology. Green genomes. Science, 332, 1372-1375.
    • (2011) Science , vol.332 , pp. 1372-1375
    • Pennisi, E.1
  • 54
    • 27244444717 scopus 로고    scopus 로고
    • The UGT73C5 of A. thaliana glucosylates brassinosteroids
    • Poppenberger, B., Fujioka, S., Soeno, K., et al. (2005) The UGT73C5 of A. thaliana glucosylates brassinosteroids. Proc. Natl. Acad. Sci. USA, 102, 15253-15258.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15253-15258
    • Poppenberger, B.1    Fujioka, S.2    Soeno, K.3
  • 55
    • 0035113472 scopus 로고    scopus 로고
    • Higher plant glycosyltransferases
    • reviews3004.
    • Ross, J., Li, Y., Lim, E., and, Bowles, D.J., (2001) Higher plant glycosyltransferases. Genome Biol. 2, reviews3004.
    • (2001) Genome Biol. , vol.2
    • Ross, J.1    Li, Y.2    Lim, E.3    Bowles, D.J.4
  • 56
    • 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.A., 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. 14, 899-906.
    • (2005) J. Biol. Chem. , vol.14 , pp. 899-906
    • Sawada, S.1    Suzuki, H.2    Ichimaida, F.3    Yamaguchi, M.A.4    Iwashita, T.5    Fukui, Y.6    Hemmi, H.7    Nishino, T.8    Nakayama, T.9
  • 57
    • 74549221016 scopus 로고    scopus 로고
    • Genome sequence of the palaeopolyploid soybean
    • Schmutz, J., Cannon, S.B., Schlueter, J., et al. (2010) Genome sequence of the palaeopolyploid soybean. Nature, 463, 178-183.
    • (2010) Nature , vol.463 , pp. 178-183
    • Schmutz, J.1    Cannon, S.B.2    Schlueter, J.3
  • 58
    • 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
  • 59
    • 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
  • 61
    • 34548446701 scopus 로고    scopus 로고
    • Exploring new search algorithms and hardware for phylogenetics: RAxML meets the IBM cell
    • Stamatakis, A., Blagojevic, F., Nikolopoulos, D., and, Antonopoulos, C., (2007) Exploring new search algorithms and hardware for phylogenetics: RAxML meets the IBM cell. J. VLSI Sig. Proc. Sys. 48, 271-286.
    • (2007) J. VLSI Sig. Proc. Sys. , vol.48 , pp. 271-286
    • Stamatakis, A.1    Blagojevic, F.2    Nikolopoulos, D.3    Antonopoulos, C.4
  • 62
    • 0035185811 scopus 로고    scopus 로고
    • Cloning and characterization of a bean UDP-glucosyltransferase cDNA expressed during plant-bacterial interactions
    • Sullivan, T.A., Jakobek, J.L., and, Lindgren, P.B., (2001) Cloning and characterization of a bean UDP-glucosyltransferase cDNA expressed during plant-bacterial interactions. Mol. Plant Microbe Interact. 14, 90-92.
    • (2001) Mol. Plant Microbe Interact. , vol.14 , pp. 90-92
    • Sullivan, T.A.1    Jakobek, J.L.2    Lindgren, P.B.3
  • 63
    • 38549136871 scopus 로고    scopus 로고
    • The rice annotation project database (RAP-DB): 2008 update
    • Tanaka, T., Antonio, B.A., Kikuchi, S., et al. (2008) The rice annotation project database (RAP-DB): 2008 update. Nucleic Acids Res. 36, D1028-D1033.
    • (2008) Nucleic Acids Res. , vol.36
    • Tanaka, T.1    Antonio, B.A.2    Kikuchi, S.3
  • 64
    • 17044369876 scopus 로고    scopus 로고
    • Functional genomics by integrated analysis of metabolome and transcriptome of A. thaliana plants over-expressing an MYB transcription factor
    • Tohge, T., Nishiyama, Y., Hirai, M.Y., et al. (2005) Functional genomics by integrated analysis of metabolome and transcriptome of A. thaliana plants over-expressing an MYB transcription factor. Plant J. 42, 218-235.
    • (2005) Plant J. , vol.42 , pp. 218-235
    • Tohge, T.1    Nishiyama, Y.2    Hirai, M.Y.3
  • 65
    • 33748760611 scopus 로고    scopus 로고
    • The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)
    • Tuskan, G.A., Difazio, S., Jansson, S., et al. (2006) The genome of black cottonwood, Populus trichocarpa (Torr. & Gray). Science, 313, 1596-1604.
    • (2006) Science , vol.313 , pp. 1596-1604
    • Tuskan, G.A.1    Difazio, S.2    Jansson, S.3
  • 66
    • 0037356424 scopus 로고    scopus 로고
    • O-Glucosylation of cis-zeatin in maize. Characterization of genes, enzymes, and endogenous cytokinins
    • Veach, Y.K., Martin, R.C., Mok, D.W.S., Malbec, J., Vankova, R., and, Mok, M.C., (2003) O-Glucosylation of cis-zeatin in maize. Characterization of genes, enzymes, and endogenous cytokinins. Plant Phys. 131, 1374-1380.
    • (2003) Plant Phys. , vol.131 , pp. 1374-1380
    • Veach, Y.K.1    Martin, R.C.2    Mok, D.W.S.3    Malbec, J.4    Vankova, R.5    Mok, M.C.6
  • 67
    • 77957560949 scopus 로고    scopus 로고
    • The genome of the domesticated apple (Malus × domestica Borkh.)
    • Velasco, R., Zharkikh, A., Affourtit, J., et al. (2010) The genome of the domesticated apple (Malus × domestica Borkh.). Nat. Genet. 42, 833-839.
    • (2010) Nat. Genet. , vol.42 , pp. 833-839
    • Velasco, R.1    Zharkikh, A.2    Affourtit, J.3
  • 68
    • 0030859561 scopus 로고    scopus 로고
    • Are the characteristics of betanidin glucosyltransferases from cell-suspension cultures of Dorotheanthus bellidiformis indicative of their phylogenetic relationship with flavonoid glucosyltransferases?
    • Vogt, T., Zimmermann, E., Grimm, R., Meyer, M., and, Strack, D., (1997) Are the characteristics of betanidin glucosyltransferases from cell-suspension cultures of Dorotheanthus bellidiformis indicative of their phylogenetic relationship with flavonoid glucosyltransferases? Planta, 203, 349-361.
    • (1997) Planta , vol.203 , pp. 349-361
    • Vogt, T.1    Zimmermann, E.2    Grimm, R.3    Meyer, M.4    Strack, D.5
  • 69
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A.M., Procter, J.B., Martin, D.M.A., Clamp, M., and, Barton, G.J., (2009) Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics, 25, 1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 70
    • 0033377995 scopus 로고    scopus 로고
    • Meristem-localized inducible expression of a UDP-glycosyltransferase gene is essential for growth and development in pea and alfalfa
    • Woo, H.H., Orbach, M.J., Hirsch, A.M., and, Hawes, M.C., (1999) Meristem-localized inducible expression of a UDP-glycosyltransferase gene is essential for growth and development in pea and alfalfa. Plant Cell, 11, 2303-2315.
    • (1999) Plant Cell , vol.11 , pp. 2303-2315
    • Woo, H.H.1    Orbach, M.J.2    Hirsch, A.M.3    Hawes, M.C.4
  • 71
    • 79953247573 scopus 로고    scopus 로고
    • An evolutionary view of functional diversity in family 1 glycosyltransferases
    • Yonekura-Sakakibara, K., and, Hanada, K., (2011) An evolutionary view of functional diversity in family 1 glycosyltransferases. Plant J. 66, 182-193.
    • (2011) Plant J. , vol.66 , pp. 182-193
    • Yonekura-Sakakibara, K.1    Hanada, K.2
  • 72
    • 34447502537 scopus 로고    scopus 로고
    • Identification of a flavonol 7-O-rhamnosyltransferase gene determining flavonoid pattern in A. thaliana 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 A. thaliana by transcriptome coexpression analysis and reverse genetics. J. Biol. Chem. 282, 14932-14941.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14932-14941
    • Yonekura-Sakakibara, K.1    Tohge, T.2    Niida, R.3    Saito, K.4
  • 73
    • 0037500141 scopus 로고    scopus 로고
    • Evolution by gene duplication: An update
    • Zhang, J., (2003) Evolution by gene duplication: an update. Trends Ecol. Evol. 18, 292-298.
    • (2003) Trends Ecol. Evol. , vol.18 , pp. 292-298
    • Zhang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.