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Volumn 179, Issue 3, 2010, Pages 273-280

Rice Os4BGlu12 is a wound-induced β-glucosidase that hydrolyzes cell wall-β-glucan-derived oligosaccharides and glycosides

Author keywords

Glucosidase; Cell wall; Endo (1,3 ; 1,4) glucanase; Glycosides; Rice; Wound

Indexed keywords

ESCHERICHIA COLI;

EID: 77954315904     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2010.05.013     Document Type: Article
Times cited : (28)

References (39)
  • 2
    • 0000026228 scopus 로고
    • Cyanogenesis in plants
    • Poulton J.E. Cyanogenesis in plants. J. Plant Physiol. 1990, 94:401-405.
    • (1990) J. Plant Physiol. , vol.94 , pp. 401-405
    • Poulton, J.E.1
  • 3
    • 0030198725 scopus 로고    scopus 로고
    • Diverse functions of isoflavonoids in legumes transcend antimicrobial definitions of phytoalexins
    • Dakora F.D., Phillips D.A. Diverse functions of isoflavonoids in legumes transcend antimicrobial definitions of phytoalexins. Physiol. Mol. Plant Pathol. 1996, 49:1-20.
    • (1996) Physiol. Mol. Plant Pathol. , vol.49 , pp. 1-20
    • Dakora, F.D.1    Phillips, D.A.2
  • 4
    • 33749563523 scopus 로고    scopus 로고
    • An isoflavone conjugate-hydrolyzing β-glucosidase from the roots of soybean (Glycine max) seedlings. Purification, gene cloning, phylogenetics, and cellular localization
    • Suzuki H., Takahashi S., Watanabe R., Fukushima Y., Fujita N., Noguchi A., Yokoyama R., Nishitani K., Nishino T., Nakayama T. An isoflavone conjugate-hydrolyzing β-glucosidase from the roots of soybean (Glycine max) seedlings. Purification, gene cloning, phylogenetics, and cellular localization. J. Biol. Chem. 2006, 281:30251-30259.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30251-30259
    • Suzuki, H.1    Takahashi, S.2    Watanabe, R.3    Fukushima, Y.4    Fujita, N.5    Noguchi, A.6    Yokoyama, R.7    Nishitani, K.8    Nishino, T.9    Nakayama, T.10
  • 5
    • 0000563099 scopus 로고
    • Hydrolysis of conjugated gibberellins by β-glucosidases from dwarf rice (Oryza sativa L. cv. Tan-ginbozu)
    • Schliemann W. Hydrolysis of conjugated gibberellins by β-glucosidases from dwarf rice (Oryza sativa L. cv. Tan-ginbozu). J. Plant Physiol. 1984, 116:123-132.
    • (1984) J. Plant Physiol. , vol.116 , pp. 123-132
    • Schliemann, W.1
  • 6
    • 0033213126 scopus 로고    scopus 로고
    • Expression, single-step purification, and matrix-assisted refolding of a maize cytokinin glucoside-specific β-glucosidase
    • Zouhar J., Nanak E., Brzobohaty B. Expression, single-step purification, and matrix-assisted refolding of a maize cytokinin glucoside-specific β-glucosidase. Protein Exp. Purif. 1999, 17:153-162.
    • (1999) Protein Exp. Purif. , vol.17 , pp. 153-162
    • Zouhar, J.1    Nanak, E.2    Brzobohaty, B.3
  • 7
    • 0029240490 scopus 로고
    • A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin
    • Dharmawardhana D.P., Ellis B.E., Carlson J.E. A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin. Plant Physiol. 1995, 107:331-339.
    • (1995) Plant Physiol. , vol.107 , pp. 331-339
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 8
    • 0029012960 scopus 로고
    • Biochemical and molecular characterization of barley seed β-glucosidases
    • Leah R., Kigel J., Svendsen I., Mundy J. Biochemical and molecular characterization of barley seed β-glucosidases. J. Biol. Chem. 1995, 270:15789-15797.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15789-15797
    • Leah, R.1    Kigel, J.2    Svendsen, I.3    Mundy, J.4
  • 9
    • 0032076141 scopus 로고    scopus 로고
    • A cell wall-bound β-glucosidase from germinated rice: purification and properties
    • Akiyama T., Kaku H., Shibuya N. A cell wall-bound β-glucosidase from germinated rice: purification and properties. Phytochemistry 1998, 48:49-54.
    • (1998) Phytochemistry , vol.48 , pp. 49-54
    • Akiyama, T.1    Kaku, H.2    Shibuya, N.3
  • 10
    • 12844283942 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons
    • Barleben L., Ma X., Koepke J., Peng G., Michel H., Stöckigt J. Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Biochim. Biophys. Acta 2005, 1747:89-92.
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 89-92
    • Barleben, L.1    Ma, X.2    Koepke, J.3    Peng, G.4    Michel, H.5    Stöckigt, J.6
  • 11
    • 0034610330 scopus 로고    scopus 로고
    • The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes
    • Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., Esen A. The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:13555-13560.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13555-13560
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Bevan, D.R.4    Henrissat, B.5    Esen, A.6
  • 16
    • 70349221692 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides
    • Seshadri S., Akiyama T., Opassiri R., Kuaprasert B., Ketudat Cairns J. Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides. Plant Physiol. 2009, 151:47-58.
    • (2009) Plant Physiol. , vol.151 , pp. 47-58
    • Seshadri, S.1    Akiyama, T.2    Opassiri, R.3    Kuaprasert, B.4    Ketudat Cairns, J.5
  • 18
    • 27344438757 scopus 로고    scopus 로고
    • Construction of suppression subtractive hybridization libraries and identification of brown planthopper-induced genes
    • Wang X., He R., He G. Construction of suppression subtractive hybridization libraries and identification of brown planthopper-induced genes. J. Plant Physiol. 2005, 162:1254-1262.
    • (2005) J. Plant Physiol. , vol.162 , pp. 1254-1262
    • Wang, X.1    He, R.2    He, G.3
  • 19
    • 70349479216 scopus 로고    scopus 로고
    • Expression of an endo-(1,3;1,4)-β-glucanase in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings
    • Akiyama T., Jin S., Yoshida M., Hoshino T., Opassiri R., Ketudat Cairns J.R. Expression of an endo-(1,3;1,4)-β-glucanase in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings. J. Plant Physiol. 2009, 166:1814-1825.
    • (2009) J. Plant Physiol. , vol.166 , pp. 1814-1825
    • Akiyama, T.1    Jin, S.2    Yoshida, M.3    Hoshino, T.4    Opassiri, R.5    Ketudat Cairns, J.R.6
  • 20
    • 0030138199 scopus 로고    scopus 로고
    • Visualization of differential gene expression using novel method of RNA fingerprinting based on AFLP: analysis of gene expression during potato tuber development
    • Bachem C.W., van der Hoeven R.S., de Bruijin S.M., Vreugdenhil D., Zabeau M., Visser R.G. Visualization of differential gene expression using novel method of RNA fingerprinting based on AFLP: analysis of gene expression during potato tuber development. Plant J. 1996, 9:745-753.
    • (1996) Plant J. , vol.9 , pp. 745-753
    • Bachem, C.W.1    van der Hoeven, R.S.2    de Bruijin, S.M.3    Vreugdenhil, D.4    Zabeau, M.5    Visser, R.G.6
  • 22
    • 0031052854 scopus 로고    scopus 로고
    • Purification and characterization of a (1→3)-β-d-glucan endohydrolase from rice (Oryza sativa) bran
    • Akiyama T., Shibuya N., Hrmova M., Fincher G.B. Purification and characterization of a (1→3)-β-d-glucan endohydrolase from rice (Oryza sativa) bran. Carbohydr. Res. 1997, 29:365-374.
    • (1997) Carbohydr. Res. , vol.29 , pp. 365-374
    • Akiyama, T.1    Shibuya, N.2    Hrmova, M.3    Fincher, G.B.4
  • 23
    • 33646122669 scopus 로고    scopus 로고
    • Addition of glycerol for improved methylation linkage analysis of polysaccharides
    • Kim J.S., Reuhs B.L., Michon F., Kaiser R.E., Arumugham G. Addition of glycerol for improved methylation linkage analysis of polysaccharides. Carbohydr. Res. 2006, 341:1061-1064.
    • (2006) Carbohydr. Res. , vol.341 , pp. 1061-1064
    • Kim, J.S.1    Reuhs, B.L.2    Michon, F.3    Kaiser, R.E.4    Arumugham, G.5
  • 24
    • 0015921531 scopus 로고
    • Subsite affinities of glucoamylase: examination of the validity of the subsite theory
    • Hiromi K., Nitta Y., Namura C., Ono S. Subsite affinities of glucoamylase: examination of the validity of the subsite theory. Biochim. Biophys. Acta 1973, 302:362-375.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 362-375
    • Hiromi, K.1    Nitta, Y.2    Namura, C.3    Ono, S.4
  • 25
    • 0031448747 scopus 로고    scopus 로고
    • Herbivory and caterpillar regurgitants amplify the wound-induced increases in jasmonic acid but not nicotine in Nicotiana sylvestris
    • McCloud E.S., Baldwin I.T. Herbivory and caterpillar regurgitants amplify the wound-induced increases in jasmonic acid but not nicotine in Nicotiana sylvestris. Planta 1997, 203:430-435.
    • (1997) Planta , vol.203 , pp. 430-435
    • McCloud, E.S.1    Baldwin, I.T.2
  • 26
    • 0035900389 scopus 로고    scopus 로고
    • Herbivore-induced allene oxide synthese transcripts and jasmonic acid in Nicotiana attenuata
    • Ziegler J., Keinänen M., Baldwin I.T. Herbivore-induced allene oxide synthese transcripts and jasmonic acid in Nicotiana attenuata. Phytochemistry 2001, 58:729-738.
    • (2001) Phytochemistry , vol.58 , pp. 729-738
    • Ziegler, J.1    Keinänen, M.2    Baldwin, I.T.3
  • 27
    • 34447104388 scopus 로고    scopus 로고
    • Deciphering the role of ethylene in plant-herbivore interactions
    • von Dahl C.C., Baldwin I.T. Deciphering the role of ethylene in plant-herbivore interactions. J. Plant Growth Regul. 2007, 26:201-209.
    • (2007) J. Plant Growth Regul. , vol.26 , pp. 201-209
    • von Dahl, C.C.1    Baldwin, I.T.2
  • 29
    • 0032079561 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of a barley β-d-glucosidase/(1,4)-β-d-glucan exohydrolase
    • Hrmova M., MacGregor E.A., Biely P., Stewart R.J., Fincher G.B. Substrate binding and catalytic mechanism of a barley β-d-glucosidase/(1,4)-β-d-glucan exohydrolase. J. Biol. Chem. 1998, 273:11134-11143.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11134-11143
    • Hrmova, M.1    MacGregor, E.A.2    Biely, P.3    Stewart, R.J.4    Fincher, G.B.5
  • 30
    • 33745908987 scopus 로고    scopus 로고
    • Sugar sensing and signaling in plants: conserved and novel mechanisms
    • Rolland F., Baena-Gonzalez E., Sheen J. Sugar sensing and signaling in plants: conserved and novel mechanisms. Annu. Rev. Plant Biol. 2006, 57:675-709.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 675-709
    • Rolland, F.1    Baena-Gonzalez, E.2    Sheen, J.3
  • 31
    • 36749014563 scopus 로고    scopus 로고
    • Different mechanisms for phytoalexin induction by pathogen and wound signals in Medicago truncatula
    • Naoumkina M., Farag M.A., Sumner L.W., Tang Y., Liu C.J., Dixon R.A. Different mechanisms for phytoalexin induction by pathogen and wound signals in Medicago truncatula. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:17909-17915.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17909-17915
    • Naoumkina, M.1    Farag, M.A.2    Sumner, L.W.3    Tang, Y.4    Liu, C.J.5    Dixon, R.A.6
  • 32
    • 33645211198 scopus 로고    scopus 로고
    • Reconstruction of cyanogenesis in barley (Hordeum vulgare L.) and its implications for resistance against the barley powdery mildew fungus
    • Nielsen K.A., Hrmova M., Nielsen J.N., Forslund K., Ebert S., Olsen C.E., Fincher G.B., Lindberg Möller B. Reconstruction of cyanogenesis in barley (Hordeum vulgare L.) and its implications for resistance against the barley powdery mildew fungus. Planta 2006, 223:1010-1023.
    • (2006) Planta , vol.223 , pp. 1010-1023
    • Nielsen, K.A.1    Hrmova, M.2    Nielsen, J.N.3    Forslund, K.4    Ebert, S.5    Olsen, C.E.6    Fincher, G.B.7    Lindberg Möller, B.8
  • 33
    • 33646270203 scopus 로고    scopus 로고
    • Molecular basis of substrate specificity in family 1 glycoside hydrolases
    • Marana S.R. Molecular basis of substrate specificity in family 1 glycoside hydrolases. IUBMB Life 2006, 58:63-73.
    • (2006) IUBMB Life , vol.58 , pp. 63-73
    • Marana, S.R.1
  • 34
    • 0036367181 scopus 로고    scopus 로고
    • The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda β-glycosidase
    • Marana S.R., Terra W.R., Ferreira C. The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda β-glycosidase. Eur. J. Biochem. 2002, 269:3705-3714.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3705-3714
    • Marana, S.R.1    Terra, W.R.2    Ferreira, C.3
  • 36
    • 0043092250 scopus 로고    scopus 로고
    • Mutational and structural analysis of aglycone specificity in maize and sorghum β-glucosidases
    • Verdoucq L., Czjzek M., Moriniere J., Bevan D.R., Esen A. Mutational and structural analysis of aglycone specificity in maize and sorghum β-glucosidases. J. Biol. Chem. 2003, 278:25055-25062.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25055-25062
    • Verdoucq, L.1    Czjzek, M.2    Moriniere, J.3    Bevan, D.R.4    Esen, A.5
  • 37
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Biology 1995, 3:951-960.
    • (1995) Biology , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 39
    • 0027968068 scopus 로고
    • Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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