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Volumn 66, Issue 7, 2015, Pages 2093-2106

A defence-related Olea europaea β-glucosidase hydrolyses and activates oleuropein into a potent protein cross-linking agent

Author keywords

heterologous expression; oleuropein; olive development; plant defence; protein cross linking; Glucosidase

Indexed keywords

OLEA EUROPAEA;

EID: 84928901902     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/erv002     Document Type: Article
Times cited : (42)

References (57)
  • 2
    • 84865849172 scopus 로고    scopus 로고
    • Olive phenolic compounds: Metabolic and transcriptional profiling during fruit development
    • Alagna F, Mariotti R, Panara F, et al. (2012). Olive phenolic compounds: metabolic and transcriptional profiling during fruit development. BMC Plant Biology 12, 162
    • (2012) BMC Plant Biology , vol.12 , pp. 162
    • Alagna, F.1    Mariotti, R.2    Panara, F.3
  • 4
    • 0001934743 scopus 로고
    • Accumulation of oleuropein derivatives during olive maturation
    • Amiot MJ, Fleuriet A, Macheix JJ. (1989). Accumulation of oleuropein derivatives during olive maturation. Phytochemistry 28, 67-69
    • (1989) Phytochemistry , vol.28 , pp. 67-69
    • Amiot, M.J.1    Fleuriet, A.2    MacHeix, J.J.3
  • 5
    • 78650637772 scopus 로고    scopus 로고
    • The olive DGAT2 gene is developmentally regulated and shares overlapping but Distinct expression patterns with DGAT1
    • Banilas G, Karampelias M, Makariti I, Kourti A, Hatzopoulos P. (2011). The olive DGAT2 gene is developmentally regulated and shares overlapping but Distinct expression patterns with DGAT1. Journal of Experimental Botany 62, 521-532
    • (2011) Journal of Experimental Botany , vol.62 , pp. 521-532
    • Banilas, G.1    Karampelias, M.2    Makariti, I.3    Kourti, A.4    Hatzopoulos, P.5
  • 6
    • 35748962318 scopus 로고    scopus 로고
    • Molecular architecture of strictosidine glucosidase: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family
    • Barleben L, Panjikar S, Ruppert M, Koepke J, Stockigt J. (2007). Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family. Plant Cell 19, 2886-2897
    • (2007) Plant Cell , vol.19 , pp. 2886-2897
    • Barleben, L.1    Panjikar, S.2    Ruppert, M.3    Koepke, J.4    Stockigt, J.5
  • 7
    • 0027014897 scopus 로고
    • New plant binary vectors with selectable markers located proximal to the left T-DNA border
    • Becker D, Kemper E, Schell J, Masterson R. (1992). New plant binary vectors with selectable markers located proximal to the left T-DNA border. Plant Molecular Biology 20, 1195-1197
    • (1992) Plant Molecular Biology , vol.20 , pp. 1195-1197
    • Becker, D.1    Kemper, E.2    Schell, J.3    Masterson, R.4
  • 8
    • 0011118020 scopus 로고    scopus 로고
    • Control of foodborne pathogens and spoilage microorganisms by naturally occurring antimicrobials
    • Wilson CL, ed. 2nd edn. Boca Raton, FL CRC Press
    • Beuchat LR. (2007). Control of foodborne pathogens and spoilage microorganisms by naturally occurring antimicrobials. In: Wilson CL, ed. Microbial food contamination , 2nd edn. Boca Raton, FL: CRC Press, 319-346
    • (2007) Microbial food contamination , pp. 319-346
    • Beuchat, L.R.1
  • 9
    • 0000925209 scopus 로고
    • Isolation of cornoside from Olea europaea and its transformation into halleridone
    • Bianco A, Scalzo RL, Scarpati ML. (1993). Isolation of cornoside from Olea europaea and its transformation into halleridone. Phytochemistry 32, 455-457
    • (1993) Phytochemistry , vol.32 , pp. 455-457
    • Bianco, A.1    Scalzo, R.L.2    Scarpati, M.L.3
  • 12
    • 0036100334 scopus 로고    scopus 로고
    • Changes in phenolic and enzymatic activities content during fruit ripening in two Italian cultivars of Olea europaea L
    • Briante R, Patumi M, Limongelli S, Febbraio F, Vaccaro C, Di Salle A, La Cara F, Nucci R. (2002). Changes in phenolic and enzymatic activities content during fruit ripening in two Italian cultivars of Olea europaea L Plant Science 162, 791-798
    • (2002) Plant Science , vol.162 , pp. 791-798
    • Briante, R.1    Patumi, M.2    Limongelli, S.3    Febbraio, F.4    Vaccaro, C.5    Di Salle, A.6    La Cara, F.7    Nucci, R.8
  • 13
    • 84910033124 scopus 로고    scopus 로고
    • Biological activity of oleuropein and its derivatives
    • In: Ramawat KG, Mérillon JM, eds. Berlin/Heidelberg Springer
    • Bulotta S, Oliverio M, Russo D, Procopio A. (2013). Biological activity of oleuropein and its derivatives. In: Ramawat KG, Mérillon JM, eds. Natural products. Berlin/Heidelberg: Springer, 3605-3638
    • (2013) Natural Products , pp. 3605-3638
    • Bulotta, S.1    Oliverio, M.2    Russo, D.3    Procopio, A.4
  • 15
    • 0034610330 scopus 로고    scopus 로고
    • The mechanism of substrate (aglycone) specificity in b-glucosidases is revealed by crystal structures of mutant maize b-glucosidase-DIMBOA,-DIMBOAGlc, and-dhurrin complexes
    • Czjzek M, Cicek M, Zamboni V, BeVan DR, Henrissat B, Esen A. (2000). The mechanism of substrate (aglycone) specificity in b-glucosidases is revealed by crystal structures of mutant maize b-glucosidase-DIMBOA,-DIMBOAGlc, and-dhurrin complexes. Proceedings of the National Academy of Sciences, USA 97, 13555-13560
    • (2000) Proceedings of the National Academy of Sciences, USA , 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
    • 0031002434 scopus 로고    scopus 로고
    • Direct identification of phenolic glucosides from olive leaf extracts by atmospheric pressure ionization tandem mass spectrometry
    • De Nino A, Lombardo N, Perri E, Procopio A, Raffaelli A, Sindona G. (1997). Direct identification of phenolic glucosides from olive leaf extracts by atmospheric pressure ionization tandem mass spectrometry. Journal of Mass Spectrometry 32, 533-541
    • (1997) Journal of Mass Spectrometry , vol.32 , pp. 533-541
    • De Nino, A.1    Lombardo, N.2    Perri, E.3    Procopio, A.4    Raffaelli, A.5    Sindona, G.6
  • 17
    • 0034082858 scopus 로고    scopus 로고
    • Extracellular b-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves
    • Dietz KJ, Sauter A, Wichert K, Messdaghi D, Hartung W. (2000). Extracellular b-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves. Journal of Experimental Botany 51, 937-944
    • (2000) Journal of Experimental Botany , vol.51 , pp. 937-944
    • Dietz, K.J.1    Sauter, A.2    Wichert, K.3    Messdaghi, D.4    Hartung, W.5
  • 19
    • 79958834456 scopus 로고    scopus 로고
    • Hydrophilic antioxidants of virgin olive oil. Part 2: Biosynthesis and biotransformation of phenolic compounds in virgin olive oil as affected by agronomic and processing factors
    • El Riachy M, Priego-Capote F, León L, Rallo L, de Castro L, Dolores M. (2011). Hydrophilic antioxidants of virgin olive oil. Part 2: Biosynthesis and biotransformation of phenolic compounds in virgin olive oil as affected by agronomic and processing factors. European Journal of Lipid Science and Technology 113, 692-707
    • (2011) European Journal of Lipid Science and Technology , vol.113 , pp. 692-707
    • El Riachy, M.1    Priego-Capote, F.2    León, L.3    Rallo, L.4    De Castro, L.5    Dolores, M.6
  • 21
    • 0039596881 scopus 로고    scopus 로고
    • Molecular cloning and analysis of strictosidine b-d-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus
    • Geerlings A, Ibanez M, Memelink J, Van Der Heijden R, Verpoorte R. (2000). Molecular cloning and analysis of strictosidine b-d-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus. Journal of Biological Chemistry 275, 3051-3056
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 3051-3056
    • Geerlings, A.1    Ibanez, M.2    Memelink, J.3    Van Der Heijden, R.4    Verpoorte, R.5
  • 24
    • 84860436233 scopus 로고    scopus 로고
    • B-Glucosidase involvement in the formation and transformation of oleuropein during the growth and development of olive fruits (Olea europaea L cv Arbequina) grown under different farming practices
    • Gutierrez-Rosales F, Romero MP, Casanovas M, Motilva MJ, Mínguez-Mosquera MI. (2012). b-Glucosidase involvement in the formation and transformation of oleuropein during the growth and development of olive fruits (Olea europaea L cv Arbequina) grown under different farming practices. Journal of Agricultural and Food Chemistry 60, 4348-4358
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 4348-4358
    • Gutierrez-Rosales, F.1    Romero, M.P.2    Casanovas, M.3    Motilva, M.J.4    Mínguez-Mosquera, M.I.5
  • 26
    • 0019322070 scopus 로고
    • Glucosidases involved in indole alkaloid biosynthesis of Catharanthus cell cultures
    • Hemscheidt T, Zenk MH. (1980). Glucosidases involved in indole alkaloid biosynthesis of Catharanthus cell cultures. FEBS Letters 110, 187-191
    • (1980) FEBS Letters , vol.110 , pp. 187-191
    • Hemscheidt, T.1    Zenk, M.H.2
  • 27
    • 0006894477 scopus 로고
    • The aglycone specificity of plant b-glycosidases
    • Hösel W, Conn EE. (1982). The aglycone specificity of plant b-glycosidases. Trends in Biochemical Sciences 7, 219-221
    • (1982) Trends in Biochemical Sciences , vol.7 , pp. 219-221
    • Hösel, W.1    Conn, E.E.2
  • 29
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • Kozak M. (1984). Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Research 12, 857-872
    • (1984) Nucleic Acids Research , vol.12 , pp. 857-872
    • Kozak, M.1
  • 30
    • 0034015983 scopus 로고    scopus 로고
    • Developmental regulation of the maize Zm-p60.1 gene encoding a b-glucosidase located to plastids
    • Kristoffersen P, Brzobohaty B, Höhfeld I, Bako L, Melkonian M, Palme K. (2000). Developmental regulation of the maize Zm-p60.1 gene encoding a b-glucosidase located to plastids. Planta 210, 407-415
    • (2000) Planta , vol.210 , pp. 407-415
    • Kristoffersen, P.1    Brzobohaty, B.2    Höhfeld, I.3    Bako, L.4    Melkonian, M.5    Palme, K.6
  • 34
    • 33749524551 scopus 로고    scopus 로고
    • Changes in oleuropein levels during differentiation and development of floral buds in 'Arbequina' olives
    • Malik NS, Bradford JM. (2006). Changes in oleuropein levels during differentiation and development of floral buds in 'Arbequina' olives. Scientia Horticulturae 110, 274-278
    • (2006) Scientia Horticulturae , vol.110 , pp. 274-278
    • Malik, N.S.1    Bradford, J.M.2
  • 35
    • 79960279363 scopus 로고    scopus 로고
    • Cold affects the transcription of fatty acid desaturases and oil quality in the fruit of Olea europaea L genotypes with different cold hardiness
    • Matteucci M, D'angeli S, Errico S, Lamanna R, Perrotta G, Altamura MM. (2011). Cold affects the transcription of fatty acid desaturases and oil quality in the fruit of Olea europaea L genotypes with different cold hardiness. Journal of Experimental Botany 62, 3403-3420
    • (2011) Journal of Experimental Botany , vol.62 , pp. 3403-3420
    • Matteucci, M.1    D'angeli, S.2    Errico, S.3    Lamanna, R.4    Perrotta, G.5    Altamura, M.M.6
  • 36
    • 33749678036 scopus 로고    scopus 로고
    • Cell and tissue localization of b-glucosidase during the ripening of olive fruit (Olea europaea) by in situ activity assay
    • Mazzuca S, Spadafora A, Innocenti AM. (2006). Cell and tissue localization of b-glucosidase during the ripening of olive fruit (Olea europaea) by in situ activity assay. Plant Science 171, 726-733
    • (2006) Plant Science , vol.171 , pp. 726-733
    • Mazzuca, S.1    Spadafora, A.2    Innocenti, A.M.3
  • 37
    • 4644254272 scopus 로고    scopus 로고
    • Effect of the maturation process of the olive fruit on the phenolic fraction of drupes and oils from Arbequina, Farga, and Morrut cultivars
    • Morelló JR, Romero MP, Motilva MJ. (2004). Effect of the maturation process of the olive fruit on the phenolic fraction of drupes and oils from Arbequina, Farga, and Morrut cultivars. Journal of Agricultural and Food Chemistry 52, 6002-6009
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 6002-6009
    • Morelló, J.R.1    Romero, M.P.2    Motilva, M.J.3
  • 39
    • 77954643863 scopus 로고    scopus 로고
    • Oleuropein in olive and its pharmacological effects
    • Omar SH. (2010). Oleuropein in olive and its pharmacological effects. Scientia Pharmaceutica 78, 133-154
    • (2010) Scientia Pharmaceutica , vol.78 , pp. 133-154
    • Omar, S.H.1
  • 40
    • 77957330505 scopus 로고    scopus 로고
    • HPLC analysis of oleuropein, hydroxytyrosol, and tyrosol in stems and roots of Olea europaea L cv Picual during ripening
    • Ortega-García F, Peragón J. (2010). HPLC analysis of oleuropein, hydroxytyrosol, and tyrosol in stems and roots of Olea europaea L cv Picual during ripening. Journal of the Science of Food and Agriculture 90, 2295-2300
    • (2010) Journal of the Science of Food and Agriculture , vol.90 , pp. 2295-2300
    • Ortega-García, F.1    Peragón, J.2
  • 41
    • 84885181609 scopus 로고    scopus 로고
    • Role of plant b-glucosidases in the dual defence system of iridoid glycosides and their hydrolyzing enzymes in Plantago lanceolata and Plantago major
    • Pankoke H, Buschmann T, Müller C. (2013). Role of plant b-glucosidases in the dual defence system of iridoid glycosides and their hydrolyzing enzymes in Plantago lanceolata and Plantago major. Phytochemistry 94, 99-107
    • (2013) Phytochemistry , vol.94 , pp. 99-107
    • Pankoke, H.1    Buschmann, T.2    Müller, C.3
  • 42
    • 84889795035 scopus 로고    scopus 로고
    • Comparative transcriptional profiling analysis of olive ripe-fruit pericarp and abscission zone tissues shows expression differences and distinct patterns of transcriptional regulation
    • Parra R, Paredes M, Sanchez-Calle I, Gomez-Jimenez M. (2013). Comparative transcriptional profiling analysis of olive ripe-fruit pericarp and abscission zone tissues shows expression differences and distinct patterns of transcriptional regulation. BMC Genomics 14, 866
    • (2013) BMC Genomics , vol.14 , pp. 866
    • Parra, R.1    Paredes, M.2    Sanchez-Calle, I.3    Gomez-Jimenez, M.4
  • 43
    • 69949126926 scopus 로고    scopus 로고
    • Purification and characterization of an olive fruit b-glucosidase involved in the biosynthesis of virgin olive oil phenolics
    • Romero-Segura C, Sanz C, Perez AG. (2009). Purification and characterization of an olive fruit b-glucosidase involved in the biosynthesis of virgin olive oil phenolics. Journal of Agricultural and Food Chemistry 57, 7983-7988
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 7983-7988
    • Romero-Segura, C.1    Sanz, C.2    Perez, A.G.3
  • 44
    • 0037462015 scopus 로고    scopus 로고
    • Quantitative changes in phenolic content during physiological development of the olive (Olea europaea) cultivar Hardy's Mammoth
    • Ryan D, Prenzler PD, Lavee S, Antolovich M, Robards K. (2003). Quantitative changes in phenolic content during physiological development of the olive (Olea europaea) cultivar Hardy's Mammoth. Journal of Agricultural and Food Chemistry 51, 2532-2538
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 2532-2538
    • Ryan, D.1    Prenzler, P.D.2    Lavee, S.3    Antolovich, M.4    Robards, K.5
  • 45
    • 84868691654 scopus 로고    scopus 로고
    • Genetic responses induced in olive roots upon colonization by the biocontrol endophytic bacterium Pseudomonas fluorescens PICF7
    • Schiliró E, Ferrara M, Nigro F, Mercado-Blanco J. (2012). Genetic responses induced in olive roots upon colonization by the biocontrol endophytic bacterium Pseudomonas fluorescens PICF7. PLoS One 7, e48646
    • (2012) PLoS One , vol.7 , pp. e48646
    • Schiliró, E.1    Ferrara, M.2    Nigro, F.3    Mercado-Blanco, J.4
  • 46
    • 0022586609 scopus 로고
    • Partial purification and characterization of raucaffricine b-d-glucosidase from plant cellsuspension cultures of Rauwolfia serpentina BENTH
    • Schübel H, Stöckigt J, Feicht R, Simon H. (1986). Partial purification and characterization of raucaffricine b-d-glucosidase from plant cellsuspension cultures of Rauwolfia serpentina BENTH. Helvetica Chimica Acta 69, 538-547
    • (1986) Helvetica Chimica Acta , vol.69 , pp. 538-547
    • Schübel, H.1    Stöckigt, J.2    Feicht, R.3    Simon, H.4
  • 48
    • 70349221692 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Os3BGlu6, a rice b-glucosidase hydrolyzing hydrophobic glycosides and (1?3)-And (1?2)-linked disaccharides
    • Seshadri S, Akiyama T, Opassiri R, Kuaprasert B, Cairns JK. (2009). Structural and enzymatic characterization of Os3BGlu6, a rice b-glucosidase hydrolyzing hydrophobic glycosides and (1?3)-And (1?2)-linked disaccharides. Plant Physiology 151, 47-58
    • (2009) Plant Physiology , vol.151 , pp. 47-58
    • Seshadri, S.1    Akiyama, T.2    Opassiri, R.3    Kuaprasert, B.4    Cairns, J.K.5
  • 50
    • 0043092250 scopus 로고    scopus 로고
    • Mutational and structural analysis of aglycone specificity in maize and sorghum b-glucosidases
    • Verdoucq L, Czjzek M, Moriniere J, BeVan DR, Esen A. (2003). Mutational and structural analysis of aglycone specificity in maize and sorghum b-glucosidases. Journal of Biological Chemistry , 278, 25055-25062
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 25055-25062
    • Verdoucq, L.1    Czjzek, M.2    Moriniere, J.3    Bevan, D.R.4    Esen, A.5
  • 51
    • 3843105862 scopus 로고    scopus 로고
    • Structural determinants of substrate specificity in family 1 b-glucosidases: Novel insights from the crystal structure of sorghum dhurrinase-1, a plant b-glucosidase with strict specificity, in complex with its natural substrate
    • Verdoucq L, Morinière J, BeVan DR, Esen A, Vasella A, Henrissat B, Czjze M. (2004). Structural determinants of substrate specificity in family 1 b-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant b-glucosidase with strict specificity, in complex with its natural substrate. Journal of Biological Chemistry 279, 31796-31803
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 31796-31803
    • Verdoucq, L.1    Morinière, J.2    Bevan, D.R.3    Esen, A.4    Vasella, A.5    Henrissat, B.6    Czjze, M.7
  • 52
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet O, Rivas S, Mestre P, Baulcombe D. (2003). An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. The Plant Journal 33, 949-956
    • (2003) The Plant Journal , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 53
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis b-glucosidase by kinetic analysis of mutants
    • Wang Q, Trimbur D, Graham R, Warren R, Withers S. (1995). Identification of the acid/base catalyst in Agrobacterium faecalis b-glucosidase by kinetic analysis of mutants. Biochemistry 34, 14554-14562
    • (1995) Biochemistry , vol.34 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.4    Withers, S.5
  • 54
    • 62949139001 scopus 로고    scopus 로고
    • Developmental expression of b-glucosidase in olive leaves
    • Wang W, Li C, Hu X. (2009). Developmental expression of b-glucosidase in olive leaves. Biologia Plantarum 53, 138-140
    • (2009) Biologia Plantarum , vol.53 , pp. 138-140
    • Wang, W.1    Li, C.2    Hu, X.3
  • 55
    • 0029645415 scopus 로고
    • The threedimensional structure of 6-phospho-b-galactosidase from Lactococcus lactis
    • Wiesmann C, Beste G, Hengstenberg W, Schulz GE. (1995). The threedimensional structure of 6-phospho-b-galactosidase from Lactococcus lactis. Structure 3, 961-968
    • (1995) Structure , vol.3 , pp. 961-968
    • Wiesmann, C.1    Beste, G.2    Hengstenberg, W.3    Schulz, G.E.4
  • 56
    • 79960722964 scopus 로고    scopus 로고
    • Insect herbivore counteradaptations to the plant glucosinolate-myrosinase system
    • Winde I, Wittstock U. (2011). Insect herbivore counteradaptations to the plant glucosinolate-myrosinase system. Phytochemistry 72, 1566-1575
    • (2011) Phytochemistry , vol.72 , pp. 1566-1575
    • Winde, I.1    Wittstock, U.2


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