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Volumn 33, Issue 5, 2011, Pages 1867-1875

Identification and partial characterization of two cysteine proteases from castor bean leaves (Ricinus communis L.) activated by wounding and methyl jasmonate stress

Author keywords

Castor bean; Cysteine protease; Mechanical wounding; Methyl jasmonate; Ricinus communis

Indexed keywords

RICINUS COMMUNIS;

EID: 80051672998     PISSN: 01375881     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11738-011-0730-z     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 60349085071 scopus 로고    scopus 로고
    • Methyl jasmonate differentially affects tocopherol content and tyrosine amino transferase activity in cultured cells of Amaranthus caudatus and Chenopodium quinoa
    • Antognoni M, Faudale F, Poli S, Biondi F (2008) Methyl jasmonate differentially affects tocopherol content and tyrosine amino transferase activity in cultured cells of Amaranthus caudatus and Chenopodium quinoa. Plant Biol 11: 161-169.
    • (2008) Plant Biol , vol.11 , pp. 161-169
    • Antognoni, M.1    Faudale, F.2    Poli, S.3    Biondi, F.4
  • 3
    • 33747040150 scopus 로고    scopus 로고
    • Effects of mechanical wounding on Carica papaya cysteine endopeptidases accumulation and activity
    • Azarkan M, Dibiani R, Baulard C, Baeyens-Volant D (2006) Effects of mechanical wounding on Carica papaya cysteine endopeptidases accumulation and activity. Int J Biol Macromol 38: 216-224.
    • (2006) Int J Biol Macromol , vol.38 , pp. 216-224
    • Azarkan, M.1    Dibiani, R.2    Baulard, C.3    Baeyens-Volant, D.4
  • 4
    • 0017184389 scopus 로고
    • A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0032811716 scopus 로고    scopus 로고
    • Methyl jasmonate changes the levels of rubisco and other leaf proteins in Ricinus communis
    • Cavalcante APR, Jacinto T, Machado OLT (1999) Methyl jasmonate changes the levels of rubisco and other leaf proteins in Ricinus communis. Acta Physiol Plant 21: 161-166.
    • (1999) Acta Physiol Plant , vol.21 , pp. 161-166
    • Cavalcante, A.P.R.1    Jacinto, T.2    Machado, O.L.T.3
  • 6
    • 0036749805 scopus 로고    scopus 로고
    • Molecular characterization of a senescence-associated gene encoding cysteine proteinase and its gene expression during leaf senescence in sweet potato
    • Chen GH, Huang LT, Yap MN, Lee RH, Huang YJ, Cheng MC, Chen SCG (2002) Molecular characterization of a senescence-associated gene encoding cysteine proteinase and its gene expression during leaf senescence in sweet potato. Plant Cell Physiol 43: 984-991.
    • (2002) Plant Cell Physiol , vol.43 , pp. 984-991
    • Chen, G.H.1    Huang, L.T.2    Yap, M.N.3    Lee, R.H.4    Huang, Y.J.5    Cheng, M.C.6    Chen, S.C.G.7
  • 7
    • 77953131348 scopus 로고    scopus 로고
    • Expression of sweet potato cysteine protease SPCP2 altered developmental characteristics and stress responses in transgenic Arabidopsis plants
    • Chen H-J, Su C-T, Lin C-H, Huang G-J, Lin Y-H (2010) Expression of sweet potato cysteine protease SPCP2 altered developmental characteristics and stress responses in transgenic Arabidopsis plants. J Plant Physiol 167: 838-847.
    • (2010) J Plant Physiol , vol.167 , pp. 838-847
    • Chen, H.-J.1    Su, C.-T.2    Lin, C.-H.3    Huang, G.-J.4    Lin, Y.-H.5
  • 8
    • 0038709697 scopus 로고    scopus 로고
    • The oxylipin pathway in Arabidopsis
    • C. R. Somerville and E. M. Meyerowitz (Eds.), Rockville: American Society of Plant Biologists
    • Creelman RA, Rao MV (2002) The oxylipin pathway in Arabidopsis. In: Somerville CR, Meyerowitz EM (eds) The arabidopsis book. American Society of Plant Biologists, Rockville, pp 1-24.
    • (2002) The Arabidopsis Book , pp. 1-24
    • Creelman, R.A.1    Rao, M.V.2
  • 9
    • 27744593837 scopus 로고    scopus 로고
    • Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)
    • Damle MS, Giri AP, Sainani MN, Gupta VS (2005) Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree). Phytochemistry 66: 2659-2667.
    • (2005) Phytochemistry , vol.66 , pp. 2659-2667
    • Damle, M.S.1    Giri, A.P.2    Sainani, M.N.3    Gupta, V.S.4
  • 10
    • 0028139552 scopus 로고
    • 3-induced degradation of Rubisco protein and loss of Rubisco mRNA in relation to leaf age in Solanum tuberosum L
    • 3-induced degradation of Rubisco protein and loss of Rubisco mRNA in relation to leaf age in Solanum tuberosum L. New Phytol 127: 741-748.
    • (1994) New Phytol , vol.127 , pp. 741-748
    • Eckardt, N.A.1    Pell, E.J.2
  • 11
    • 0026754798 scopus 로고
    • Sulfur starvation in Lemna leads to degradation of ribulose-bisphosphate carboxylase without plant death
    • Ferreira RMB, Teixeira ARN (1992) Sulfur starvation in Lemna leads to degradation of ribulose-bisphosphate carboxylase without plant death. J Biol Chem 267: 7253-7257.
    • (1992) J Biol Chem , vol.267 , pp. 7253-7257
    • Ferreira, R.M.B.1    Teixeira, A.R.N.2
  • 12
    • 0032483470 scopus 로고    scopus 로고
    • Induction of a cysteine protease cDNA from Mesembryanthemum crystallinum leaves by environmental stress and plant growth regulators
    • Forsthoefel NR, Cushman MAF, Ostrem JA, Cushman JC (1998) Induction of a cysteine protease cDNA from Mesembryanthemum crystallinum leaves by environmental stress and plant growth regulators. Plant Sci 136: 195-206.
    • (1998) Plant Sci , vol.136 , pp. 195-206
    • Forsthoefel, N.R.1    Cushman, M.A.F.2    Ostrem, J.A.3    Cushman, J.C.4
  • 13
    • 33644853519 scopus 로고    scopus 로고
    • Role of two cysteine proteinases in the susceptible response of Nicotiana benthamiana to Colletotrichum destructivum and the hypersensitive response to Pseudomonas syringae pv. tomato
    • Hao L, Hsiang T, Goodwin PH (2006) Role of two cysteine proteinases in the susceptible response of Nicotiana benthamiana to Colletotrichum destructivum and the hypersensitive response to Pseudomonas syringae pv. tomato. Plant Sci 170: 1001-1009.
    • (2006) Plant Sci , vol.170 , pp. 1001-1009
    • Hao, L.1    Hsiang, T.2    Goodwin, P.H.3
  • 14
    • 4243132867 scopus 로고    scopus 로고
    • Different classes of proteases are involved in the response to drought of Phaseolus vulgaris L. cultivars differing in sensitivity
    • Hieng B, Ugrinovic K, Sustar-Vozlic J, Kidric M (2004) Different classes of proteases are involved in the response to drought of Phaseolus vulgaris L. cultivars differing in sensitivity. J Plant Physiol 161: 519-530.
    • (2004) J Plant Physiol , vol.161 , pp. 519-530
    • Hieng, B.1    Ugrinovic, K.2    Sustar-Vozlic, J.3    Kidric, M.4
  • 16
    • 1042290220 scopus 로고    scopus 로고
    • Papain protects papaya trees from herbovirous insects: role of cysteine proteases in latex
    • Kono K, Hirayama C, Nakamura M, Tateishi K, Tamura Y, Hattori M, Kohno K (2004) Papain protects papaya trees from herbovirous insects: role of cysteine proteases in latex. Plant J 37: 370-378.
    • (2004) Plant J , vol.37 , pp. 370-378
    • Kono, K.1    Hirayama, C.2    Nakamura, M.3    Tateishi, K.4    Tamura, Y.5    Hattori, M.6    Kohno, K.7
  • 17
    • 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
  • 18
    • 0027547387 scopus 로고
    • Circadian expression and induction by wounding of tobacco genes for cysteine proteinase
    • Linthorst HLM, van der DC, Brederode FT, Bol JF et al (1993) Circadian expression and induction by wounding of tobacco genes for cysteine proteinase. Plant Mol Biol 21: 685-694.
    • (1993) Plant Mol Biol , vol.21 , pp. 685-694
    • Linthorst, H.L.M.1    van Der, D.C.2    Brederode, F.T.3    Bol, J.F.4
  • 20
    • 0026795063 scopus 로고
    • Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Mehta RA, Fawcett TW, Porath D, Mattoo AK (1992) Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1, 5-bisphosphate carboxylase/oxygenase. J Biol Chem 267: 2810-2816.
    • (1992) J Biol Chem , vol.267 , pp. 2810-2816
    • Mehta, R.A.1    Fawcett, T.W.2    Porath, D.3    Mattoo, A.K.4
  • 21
    • 1842817420 scopus 로고    scopus 로고
    • Constitutive overexpression of allene oxide cyclase in tomato (Lycopersicon esculentum cv. Lukullus) elevates levels of some jasmonates and octadecanoids in flower organs but not in leaves
    • Miersch O, Weichert H, Stenzel I, Hause B, Maucher H, Feussner I, Wasternack C (2004) Constitutive overexpression of allene oxide cyclase in tomato (Lycopersicon esculentum cv. Lukullus) elevates levels of some jasmonates and octadecanoids in flower organs but not in leaves. Phytochemistry 65: 847-856.
    • (2004) Phytochemistry , vol.65 , pp. 847-856
    • Miersch, O.1    Weichert, H.2    Stenzel, I.3    Hause, B.4    Maucher, H.5    Feussner, I.6    Wasternack, C.7
  • 23
    • 36348932196 scopus 로고    scopus 로고
    • Systemic wound signaling in tomato leaves is cooperatively regulated by systemin and hydroxyproline-rich glycopeptides signals
    • Narváz-Vásquez J, Orozco-Cárdenas ML, Ryan CA (2007) Systemic wound signaling in tomato leaves is cooperatively regulated by systemin and hydroxyproline-rich glycopeptides signals. Plant Mol Biol 65: 711-718.
    • (2007) Plant Mol Biol , vol.65 , pp. 711-718
    • Narváz-Vásquez, J.1    Orozco-Cárdenas, M.L.2    Ryan, C.A.3
  • 24
    • 0027490705 scopus 로고
    • Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon exculentum (tomato)
    • Pautot V, Holze FM, Reisch B, Walling LL (1993) Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon exculentum (tomato). PNAS 90: 9906-9910.
    • (1993) Pnas , vol.90 , pp. 9906-9910
    • Pautot, V.1    Holze, F.M.2    Reisch, B.3    Walling, L.L.4
  • 25
    • 0035940404 scopus 로고    scopus 로고
    • Production of multiple plant hormones from a single polyprotein precursor
    • Pearce G, Moura DS, Stratmann J, Ryan CA (2001) Production of multiple plant hormones from a single polyprotein precursor. PNAS 98: 12843-12847.
    • (2001) Pnas , vol.98 , pp. 12843-12847
    • Pearce, G.1    Moura, D.S.2    Stratmann, J.3    Ryan, C.A.4
  • 26
    • 0035983830 scopus 로고    scopus 로고
    • Accumulation of chloroplast-targeted lipoxygenase in passion fruit leaves in response to methyl jasmonate
    • Rangel M, Machado OLT, da Cunha M, Jacinto T (2002) Accumulation of chloroplast-targeted lipoxygenase in passion fruit leaves in response to methyl jasmonate. Phytochemistry 60: 619-625.
    • (2002) Phytochemistry , vol.60 , pp. 619-625
    • Rangel, M.1    Machado, O.L.T.2    da Cunha, M.3    Jacinto, T.4
  • 27
    • 0033105962 scopus 로고    scopus 로고
    • Protein purification from polyacrylamide gels by sonication extraction
    • Retamal CA, Thiebaut P, Alves EW (1999) Protein purification from polyacrylamide gels by sonication extraction. Anal Biochem 268: 15-20.
    • (1999) Anal Biochem , vol.268 , pp. 15-20
    • Retamal, C.A.1    Thiebaut, P.2    Alves, E.W.3
  • 28
    • 0034615558 scopus 로고    scopus 로고
    • The systemin signaling pathway: differential activation of plant defensive genes
    • Ryan CA (2000) The systemin signaling pathway: differential activation of plant defensive genes. Biochim Biophys Acta 1477: 112-121.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 112-121
    • Ryan, C.A.1
  • 29
    • 51249107963 scopus 로고    scopus 로고
    • Plant cysteine proteinases: evaluation of the pharmacological activity
    • Salas CE, Gomes MTR, Hernandez M, Lopes MTP (2008) Plant cysteine proteinases: evaluation of the pharmacological activity. Phytochemistry 69: 2263-2269.
    • (2008) Phytochemistry , vol.69 , pp. 2263-2269
    • Salas, C.E.1    Gomes, M.T.R.2    Hernandez, M.3    Lopes, M.T.P.4
  • 30
    • 0344045677 scopus 로고
    • Transcriptional activation by heat and cold of a thiol protease gene in tomato
    • Schaffer MA, Fischer RL (1990) Transcriptional activation by heat and cold of a thiol protease gene in tomato. Plant Physiol 93: 1486-1491.
    • (1990) Plant Physiol , vol.93 , pp. 1486-1491
    • Schaffer, M.A.1    Fischer, R.L.2
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 32
    • 0032007668 scopus 로고    scopus 로고
    • Action of proteolysis-resistant systemin analogues in wound signalling
    • Schaller A et al (1998) Action of proteolysis-resistant systemin analogues in wound signalling. Phytochemistry 47: 605-612.
    • (1998) Phytochemistry , vol.47 , pp. 605-612
    • Schaller, A.1
  • 33
    • 0028446555 scopus 로고
    • Vacuolar. Processing enzyme of soybean that converts proprotein to the corresponding mature forms
    • Shimada T, Hiraiwa N, Nishimura M, Hara-Nishimura I (1994) Vacuolar. Processing enzyme of soybean that converts proprotein to the corresponding mature forms. Plant Cell Physiol 35: 713-718.
    • (1994) Plant Cell Physiol , vol.35 , pp. 713-718
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 34
    • 76949094781 scopus 로고    scopus 로고
    • Pergularain e I'-a plant cysteine protease with thrombin-like activity from Pergularia extensa latex
    • Shivaprasad HV, Rajaiah R, Frey BM, Frey FJ, Vishwanath BS (2010) Pergularain e I'-a plant cysteine protease with thrombin-like activity from Pergularia extensa latex. Thromb Res 125: 100-105.
    • (2010) Thromb Res , vol.125 , pp. 100-105
    • Shivaprasad, H.V.1    Rajaiah, R.2    Frey, B.M.3    Frey, F.J.4    Vishwanath, B.S.5
  • 35
    • 77649191097 scopus 로고    scopus 로고
    • Proteolytic activity and cysteine protease expression in wheat leaves under severe soil drought and recovery
    • Simova-Stoilova L, Vaseva I, Grigorova B, Demirevska K, Feller U (2010) Proteolytic activity and cysteine protease expression in wheat leaves under severe soil drought and recovery. Plant Physiol Biochem 48: 200-206.
    • (2010) Plant Physiol Biochem , vol.48 , pp. 200-206
    • Simova-Stoilova, L.1    Vaseva, I.2    Grigorova, B.3    Demirevska, K.4    Feller, U.5
  • 36
    • 45149120488 scopus 로고    scopus 로고
    • Differential effects of methyl jasmonate on growth and division of etiolated zucchini cotyledons
    • Stoynova-Bakalova E, Petrov PI, Gigova L, Baskin TI (2008) Differential effects of methyl jasmonate on growth and division of etiolated zucchini cotyledons. Plant Biol 10: 476-484.
    • (2008) Plant Biol , vol.10 , pp. 476-484
    • Stoynova-Bakalova, E.1    Petrov, P.I.2    Gigova, L.3    Baskin, T.I.4
  • 37
    • 33748143931 scopus 로고    scopus 로고
    • Mastermind or minions? Cysteine proteinases in plant cell death
    • Trobacher CP, Senatore A, Greenwood JS (2006) Mastermind or minions? Cysteine proteinases in plant cell death. Can J Bot 84: 651-667.
    • (2006) Can J Bot , vol.84 , pp. 651-667
    • Trobacher, C.P.1    Senatore, A.2    Greenwood, J.S.3
  • 38
    • 57649119969 scopus 로고    scopus 로고
    • How plants cope with biotic interactions
    • van Dam NM (2008) How plants cope with biotic interactions. Plant Biol 11: 1-5.
    • (2008) Plant Biol , vol.11 , pp. 1-5
    • van Dam, N.M.1
  • 41
    • 57649171450 scopus 로고    scopus 로고
    • Characterization and cloning of cysteine protease that is induced in green leaves of barley
    • Watanabe Y, Matsushima S, Yamaguchi A, Shioi Y (2009) Characterization and cloning of cysteine protease that is induced in green leaves of barley. Plant Sci 176: 264-271.
    • (2009) Plant Sci , vol.176 , pp. 264-271
    • Watanabe, Y.1    Matsushima, S.2    Yamaguchi, A.3    Shioi, Y.4


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