메뉴 건너뛰기




Volumn 98, Issue 6, 2006, Pages 1145-1153

Antifungal properties of haem peroxidase from Acorus calamus

Author keywords

Acorus calamus; Antifungal; Epidermal cells; Haem peroxidase; Hyphal inhibition; Localization; Thermal stability; Xylem lumen

Indexed keywords

ANTIFUNGAL AGENT; FUNGUS ANTIBODY; PEROXIDASE;

EID: 33845265284     PISSN: 03057364     EISSN: 10958290     Source Type: Journal    
DOI: 10.1093/aob/mcl205     Document Type: Article
Times cited : (74)

References (70)
  • 3
    • 52849098721 scopus 로고    scopus 로고
    • Analysis of rape seed napin structure and potential roles of the storage protein
    • Barciszewski J, Maciej S, Haertlé T. 2000. Analysis of rape seed napin structure and potential roles of the storage protein. Journal of Protein Chemistry 19: 249-254.
    • (2000) Journal of Protein Chemistry , vol.19 , pp. 249-254
    • Barciszewski, J.1    Maciej, S.2    Haertlé, T.3
  • 5
    • 0035173104 scopus 로고    scopus 로고
    • Molecular identification and expression of the peroxidase responsible for the oxidative burst in French bean (Phaseolus vulgaris L.) and related members of the gene family
    • Blee KA, Jupe SC, Richard G, Zimmerlin A, Davies DR, Bolwell GP. 2001. Molecular identification and expression of the peroxidase responsible for the oxidative burst in French bean (Phaseolus vulgaris L.) and related members of the gene family. Plant Molecular Biology 47: 607-620.
    • (2001) Plant Molecular Biology , vol.47 , pp. 607-620
    • Blee, K.A.1    Jupe, S.C.2    Richard, G.3    Zimmerlin, A.4    Davies, D.R.5    Bolwell, G.P.6
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantification of microgram quantitites of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72: 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0026735576 scopus 로고
    • Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: A novel, rapid defence response
    • Bradley DJ, Kjellbom P, Lamb CJ. 1992. Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defence response. Cell 70: 21-30.
    • (1992) Cell , vol.70 , pp. 21-30
    • Bradley, D.J.1    Kjellbom, P.2    Lamb, C.J.3
  • 12
    • 85055568415 scopus 로고    scopus 로고
    • Induction of peroxidase during defence against pathogens
    • Datta SK, Muthukrishnan SK, eds. New York, NY: CRC Press
    • Chittoor JM, Leach JE, White EF. 1999. Induction of peroxidase during defence against pathogens. In: Datta SK, Muthukrishnan SK, eds. Pathogenesis-related proteins in plants. New York, NY: CRC Press, 171-193.
    • (1999) Pathogenesis-related Proteins in Plants , pp. 171-193
    • Chittoor, J.M.1    Leach, J.E.2    White, E.F.3
  • 13
    • 0032161863 scopus 로고    scopus 로고
    • Purification and characterization of peroxidases correlated with lignification in poplar xylem
    • Christensen JH, Bauw G, Welinder KG, Montagu MV, Boerjan W. 1998. Purification and characterization of peroxidases correlated with lignification in poplar xylem. Plant Physiology 118: 125-135.
    • (1998) Plant Physiology , vol.118 , pp. 125-135
    • Christensen, J.H.1    Bauw, G.2    Welinder, K.G.3    Montagu, M.V.4    Boerjan, W.5
  • 14
    • 0036007895 scopus 로고    scopus 로고
    • Involvement of peroxidases in the formation of the brown coloration of heartwood in Juglans nigra
    • Dehon L, Macheix JJ, Durand M. 2002. Involvement of peroxidases in the formation of the brown coloration of heartwood in Juglans nigra. Journal of Experimental Botany 53: 303-311.
    • (2002) Journal of Experimental Botany , vol.53 , pp. 303-311
    • Dehon, L.1    Macheix, J.J.2    Durand, M.3
  • 17
    • 33845250983 scopus 로고    scopus 로고
    • Pathogenesis-related proteins: Research progress in the last 15 years
    • Edreva A. 2005. Pathogenesis-related proteins: research progress in the last 15 years. General Applied Plant Physiology 31: 105-124.
    • (2005) General Applied Plant Physiology , vol.31 , pp. 105-124
    • Edreva, A.1
  • 18
    • 0029411206 scopus 로고
    • An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins
    • Epple P, Apel K, Bohlmann H. 1995. An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. Plant Physiology 109: 813-820.
    • (1995) Plant Physiology , vol.109 , pp. 813-820
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 19
    • 0001098932 scopus 로고
    • Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue
    • Espelie KE, Franceschi VR, Kolattukudy PE. 1986. Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue. Plant Physiology 87: 487-492.
    • (1986) Plant Physiology , vol.87 , pp. 487-492
    • Espelie, K.E.1    Franceschi, V.R.2    Kolattukudy, P.E.3
  • 22
    • 49049137523 scopus 로고
    • Lignification as a mechanism for induced systemic resistance in cucumber
    • Hammerschmidt R, Kuc J. 1982. Lignification as a mechanism for induced systemic resistance in cucumber. Physiology and. Molecular Plant Patholology 20: 61-71.
    • (1982) Physiology And. Molecular Plant Patholology , vol.20 , pp. 61-71
    • Hammerschmidt, R.1    Kuc, J.2
  • 23
    • 0030266346 scopus 로고    scopus 로고
    • Resistance gene-dependent plant defence responses
    • Hammond-Kosack KE, Jones JDG. 1996. Resistance gene-dependent plant defence responses. The Plant Cell 8: 1773-1791.
    • (1996) The Plant Cell , vol.8 , pp. 1773-1791
    • Hammond-Kosack, K.E.1    Jones, J.D.G.2
  • 24
    • 2942739216 scopus 로고    scopus 로고
    • A novel rice PR10 protein, RSOsPR10, specifically induced in roots by biotic and abiotic stresses, possibly via the jasmonic acid signaling pathway
    • Hashimoto M, Kisseleva L, Sawa S, Furukawa T, Komatsu S, Koshibal T. 2004. A novel rice PR10 protein, RSOsPR10, specifically induced in roots by biotic and abiotic stresses, possibly via the jasmonic acid signaling pathway. Plant and Cell Physiology 45: 550-559.
    • (2004) Plant and Cell Physiology , vol.45 , pp. 550-559
    • Hashimoto, M.1    Kisseleva, L.2    Sawa, S.3    Furukawa, T.4    Komatsu, S.5    Koshibal, T.6
  • 27
    • 2442769271 scopus 로고    scopus 로고
    • Antifungal effects of hydrogen peroxide and peroxidase on spore germination and mycelial growth of Pseudocercospora species
    • Joseph LM, Koo TT, Man WS. 1998. Antifungal effects of hydrogen peroxide and peroxidase on spore germination and mycelial growth of Pseudocercospora species. Canadian Journal of Botany 76: 2119-2124.
    • (1998) Canadian Journal of Botany , vol.76 , pp. 2119-2124
    • Joseph, L.M.1    Koo, T.T.2    Man, W.S.3
  • 29
    • 0038378824 scopus 로고    scopus 로고
    • Roles of the reactive oxygen species-generating peroxidase reactions in plant defence and growth induction
    • Kawano T. 2003. Roles of the reactive oxygen species-generating peroxidase reactions in plant defence and growth induction. Plant Cell Reports 21: 829-837.
    • (2003) Plant Cell Reports , vol.21 , pp. 829-837
    • Kawano, T.1
  • 30
    • 0032974640 scopus 로고    scopus 로고
    • Plant pathogenesis-related proteins: Molecular mechanisms of gene expression and protein function
    • Kitajima S, Sato F. 1999. Plant pathogenesis-related proteins: molecular mechanisms of gene expression and protein function. Journal of Biochemistry 125: 1-8.
    • (1999) Journal of Biochemistry , vol.125 , pp. 1-8
    • Kitajima, S.1    Sato, F.2
  • 31
    • 0033150472 scopus 로고    scopus 로고
    • Barley coleoptile peroxidases: Purification, molecular cloning and induction by pathogens
    • Kristensen BK, Bloch H, Rasmussen SK. 1999. Barley coleoptile peroxidases: purification, molecular cloning and induction by pathogens. Plant Physiology 120: 501-512.
    • (1999) Plant Physiology , vol.120 , pp. 501-512
    • Kristensen, B.K.1    Bloch, H.2    Rasmussen, S.K.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0000155139 scopus 로고
    • Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression
    • Lagrimini LM, Burkhart W, Moyer M, Rothstein S. 1987. Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: molecular analysis and tissue-specific expression. Proceedimgs of the National Academy of Sciences of the USA 84: 7542-7546.
    • (1987) Proceedimgs of the National Academy of Sciences of the USA , vol.84 , pp. 7542-7546
    • Lagrimini, L.M.1    Burkhart, W.2    Moyer, M.3    Rothstein, S.4
  • 34
    • 85042638215 scopus 로고    scopus 로고
    • Functions and regulation of plant β-1,3-glucanases (PR-2)
    • Datta SK, Muthukrishnan S, eds. Boca Raton, FL: CRC Press
    • Leubner-Metzger G, Meins F. 1999. Functions and regulation of plant β-1,3-glucanases (PR-2). In: Datta SK, Muthukrishnan S, eds. Pathogenesis-related proteins in plants. Boca Raton, FL: CRC Press, 49-76.
    • (1999) Pathogenesis-related Proteins in Plants , pp. 49-76
    • Leubner-Metzger, G.1    Meins, F.2
  • 35
    • 0034979585 scopus 로고    scopus 로고
    • Characterization of a PR-10 pathogenesis-related gene family induced in rice during infection with Magnaporthe grisea
    • McGee JD, Hamer JE, Hodges TK. 2001. Characterization of a PR-10 pathogenesis-related gene family induced in rice during infection with Magnaporthe grisea. Molecular Plant-Microbe Interactions 14: 877-886.
    • (2001) Molecular Plant-Microbe Interactions , vol.14 , pp. 877-886
    • McGee, J.D.1    Hamer, J.E.2    Hodges, T.K.3
  • 36
    • 0033768234 scopus 로고    scopus 로고
    • Salicylic acid mediated by the oxidative burst is a key molecule in local and systemic responses of cotton challenged by an avirulent race of Xanthomonas campestris pv. malvacearum
    • Martinez C, Baccou J, Bresson E, Baissac Y, Daniel J, Jalloul A, et al. 2000. Salicylic acid mediated by the oxidative burst is a key molecule in local and systemic responses of cotton challenged by an avirulent race of Xanthomonas campestris pv. malvacearum. Plant Physiology 122: 757-766.
    • (2000) Plant Physiology , vol.122 , pp. 757-766
    • Martinez, C.1    Baccou, J.2    Bresson, E.3    Baissac, Y.4    Daniel, J.5    Jalloul, A.6
  • 37
    • 0038715037 scopus 로고    scopus 로고
    • Properties of guaiacol peroxidase activities isolated from corn root plasma membranes
    • Mika A, Luthje S. 2003. Properties of guaiacol peroxidase activities isolated from corn root plasma membranes. Plant Physiology 132: 1489-1498.
    • (2003) Plant Physiology , vol.132 , pp. 1489-1498
    • Mika, A.1    Luthje, S.2
  • 40
    • 0029294601 scopus 로고
    • Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans
    • Niderman T, Genetet I, Bruyere T, Gees R, Stintzi A, Legrand M, et al. 1995. Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans. Plant Physiology 108: 17-27.
    • (1995) Plant Physiology , vol.108 , pp. 17-27
    • Niderman, T.1    Genetet, I.2    Bruyere, T.3    Gees, R.4    Stintzi, A.5    Legrand, M.6
  • 42
    • 23944488734 scopus 로고    scopus 로고
    • Plant γ-thionins: Novel insights on the mechanism of action of a multi-functional class of defence proteins
    • Peligrini PB, Franco OL. 2005. Plant γ-thionins: novel insights on the mechanism of action of a multi-functional class of defence proteins. International Journal of Biochemistry and Cell Biology 37: 2239-2253.
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , pp. 2239-2253
    • Peligrini, P.B.1    Franco, O.L.2
  • 44
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 45
    • 0035164948 scopus 로고    scopus 로고
    • Genetic engineering of plants to enhance resistance to fungal pathogens - A review of progress and future prospects
    • Punja ZK. 2001. Genetic engineering of plants to enhance resistance to fungal pathogens - a review of progress and future prospects. Canadian Journal of Plant Pathology 23: 216-235.
    • (2001) Canadian Journal of Plant Pathology , vol.23 , pp. 216-235
    • Punja, Z.K.1
  • 46
    • 0041153898 scopus 로고    scopus 로고
    • PR-1 protein inhibits the differentiation of rust infection hyphae in leaves of acquired resistant broad bean
    • Rauscher M, Adam AL, Wirtz S, Guggenheim R, Mendgen K, Deising HB. 1999. PR-1 protein inhibits the differentiation of rust infection hyphae in leaves of acquired resistant broad bean. The Plant Journal 19: 625-633.
    • (1999) The Plant Journal , vol.19 , pp. 625-633
    • Rauscher, M.1    Adam, A.L.2    Wirtz, S.3    Guggenheim, R.4    Mendgen, K.5    Deising, H.B.6
  • 47
    • 0033814919 scopus 로고    scopus 로고
    • Purification, characterization and antifungal properties of a lipid-transfer protein from sunflower (Helianthus annuus) seeds
    • Regente MC, de la Canal L. 2000. Purification, characterization and antifungal properties of a lipid-transfer protein from sunflower (Helianthus annuus) seeds. Physiologia Plantarum 110: 158-163.
    • (2000) Physiologia Plantarum , vol.110 , pp. 158-163
    • Regente, M.C.1    De La Canal, L.2
  • 49
    • 29144435625 scopus 로고    scopus 로고
    • Wound-inducible oxidative responses in mountain birch leaves
    • Ruuhola T, Yang S. 2006. Wound-inducible oxidative responses in mountain birch leaves. Annals of Botany 97: 29-37.
    • (2006) Annals of Botany , vol.97 , pp. 29-37
    • Ruuhola, T.1    Yang, S.2
  • 51
    • 31844451140 scopus 로고    scopus 로고
    • Detection of pathogenesis-related proteins: Chitinase and β-1,3-glucanase in induced chickpea
    • Saikia R, Singh BP, Kumar R, Arora DK. 2005. Detection of pathogenesis-related proteins: chitinase and β-1,3-glucanase in induced chickpea. Current Science 89: 659-663.
    • (2005) Current Science , vol.89 , pp. 659-663
    • Saikia, R.1    Singh, B.P.2    Kumar, R.3    Arora, D.K.4
  • 54
    • 0842264046 scopus 로고    scopus 로고
    • Isolation and characterization of an RIP (Ribosome-Inactivating Protein)-like protein from tobacco with dual enzymatic activity
    • Sharma N, Park SW, Vepachedu R, Barbieri L, Ciani M, Stirpe F, et al. 2004. Isolation and characterization of an RIP (Ribosome-Inactivating Protein)-like protein from tobacco with dual enzymatic activity. Plant Physiology 134: 171-181.
    • (2004) Plant Physiology , vol.134 , pp. 171-181
    • Sharma, N.1    Park, S.W.2    Vepachedu, R.3    Barbieri, L.4    Ciani, M.5    Stirpe, F.6
  • 56
    • 0028254268 scopus 로고
    • The physiology and molecular biology of plant 1,3-β-Dglucanases and 1,3;1,4-β-D-glucanases
    • Simmons CR. 1994. The physiology and molecular biology of plant 1,3-β-Dglucanases and 1,3;1,4-β-D-glucanases. Critical Reviews in Plant Science 13: 325-387.
    • (1994) Critical Reviews in Plant Science , vol.13 , pp. 325-387
    • Simmons, C.R.1
  • 59
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • Terras FRG, Schoofs HME, Thevissen K, Osborn RW, Vanderleyden J, Cammue BPA, et al. 1993. Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiology 103: 1311-1319.
    • (1993) Plant Physiology , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.P.A.6
  • 61
    • 0032253808 scopus 로고    scopus 로고
    • Several thaumatin-like proteins bind to β-1,3-glucans
    • Trudel J, Grenier J, Potvin C, Asselin A. 1998. Several thaumatin-like proteins bind to β-1,3-glucans. Plant Physiology 118: 1431-1438.
    • (1998) Plant Physiology , vol.118 , pp. 1431-1438
    • Trudel, J.1    Grenier, J.2    Potvin, C.3    Asselin, A.4
  • 62
    • 11144245139 scopus 로고    scopus 로고
    • Role of inhibitors of proteolytic enzymes in plant defence against phytopathogenic microorganisms
    • Valueva TA, Mosolov VV. 2004. Role of inhibitors of proteolytic enzymes in plant defence against phytopathogenic microorganisms. Biochemistry (Moscow) 69: 1305-1309.
    • (2004) Biochemistry (Moscow) , vol.69 , pp. 1305-1309
    • Valueva, T.A.1    Mosolov, V.V.2
  • 63
    • 0002570240 scopus 로고
    • Regulation of changes in proteins and enzymes associated with active defence against virus infection
    • Wood RKS, ed. New York, NY: Plenum Press
    • Van Loon LC. 1982. Regulation of changes in proteins and enzymes associated with active defence against virus infection. In: Wood RKS, ed. Active defence mechanisms in plants. New York, NY: Plenum Press, 247-273.
    • (1982) Active Defence Mechanisms in Plants , pp. 247-273
    • Van Loon, L.C.1
  • 64
    • 0001376743 scopus 로고
    • Pathogenesis-related proteins
    • Van Loon LC. 1985. Pathogenesis-related proteins. Plant Molecular Biology 116: 111-116.
    • (1985) Plant Molecular Biology , vol.116 , pp. 111-116
    • Van Loon, L.C.1
  • 65
    • 85056316333 scopus 로고    scopus 로고
    • Occurrence and properties of plant pathogenesis-related proteins
    • Datta SK, Muthukrishnan S, eds. Boca Raton, FL: CRC Press
    • Van Loon LC. 1999. Occurrence and properties of plant pathogenesis-related proteins. In: Datta SK, Muthukrishnan S, eds. Pathogenesis-related proteins in plants. Boca Raton, FL: CRC Press, 1-19.
    • (1999) Pathogenesis-related Proteins in Plants , pp. 1-19
    • Van Loon, L.C.1
  • 66
    • 0030922738 scopus 로고    scopus 로고
    • Guaiacol peroxidase associated to soybean root plasma membranes oxidizes ascorbate
    • Vianello A, Zancani M, Nagy G, Macri F. 1997. Guaiacol peroxidase associated to soybean root plasma membranes oxidizes ascorbate. Journal of Plant Physiology 150: 573-577.
    • (1997) Journal of Plant Physiology , vol.150 , pp. 573-577
    • Vianello, A.1    Zancani, M.2    Nagy, G.3    Macri, F.4
  • 68
    • 0033000184 scopus 로고    scopus 로고
    • Antimicrobial activity of a porcine myeloperoxidase against plant pathogenic bacteria and fungi
    • Yang Y, Anderson, EJ. 1999. Antimicrobial activity of a porcine myeloperoxidase against plant pathogenic bacteria and fungi. Journal of Applied Microbiology 86: 211-220.
    • (1999) Journal of Applied Microbiology , vol.86 , pp. 211-220
    • Yang, Y.1    Anderson, E.J.2
  • 69
    • 0037162964 scopus 로고    scopus 로고
    • Isolation of novel peroxidase from French bean legumes and first demonstration of antifungal activity of a non-milk peroxidase
    • Ye XY, Ng TB. 2002. Isolation of novel peroxidase from French bean legumes and first demonstration of antifungal activity of a non-milk peroxidase. Life Science 71: 1667-1680.
    • (2002) Life Science , vol.71 , pp. 1667-1680
    • Ye, X.Y.1    Ng, T.B.2
  • 70
    • 0029278767 scopus 로고
    • Rice cationic peroxidase accumulates in xylem vessels during incompatible interactions with Xanthomonas oryzae pv. oryzae
    • Young SA, Guo A, Guikema JA, White FF, Leach JE. 1995. Rice cationic peroxidase accumulates in xylem vessels during incompatible interactions with Xanthomonas oryzae pv. oryzae. Plant Physiology 107: 1333-1341.
    • (1995) Plant Physiology , vol.107 , pp. 1333-1341
    • Young, S.A.1    Guo, A.2    Guikema, J.A.3    White, F.F.4    Leach, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.