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Volumn 217-218, Issue , 2014, Pages 158-175

Proteomics changes during the incompatible interaction between cowpea and Colletotrichum gloeosporioides (Penz.) Penz and Sacc

Author keywords

Anthracnose; Colletotrichum gloeosporioides; Mass spectrometry; Resistance; Two dimensional gel electrophoresis; Vigna unguiculata

Indexed keywords

PROTEOME; VEGETABLE PROTEIN;

EID: 84892463556     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2013.12.010     Document Type: Article
Times cited : (15)

References (64)
  • 2
    • 84857796981 scopus 로고    scopus 로고
    • Effect of harvest age and thermal processing on poly-γ-glutamate folates and minerals in African cowpea leaves (Vigna unguiculata)
    • Wawire M., Oey I., Mathooko F.M., Njoroge C.K., Shitanda D., Sila D., Hendrickx M. Effect of harvest age and thermal processing on poly-γ-glutamate folates and minerals in African cowpea leaves (Vigna unguiculata). J. Food Compos. Anal. 2012, 25:160-165.
    • (2012) J. Food Compos. Anal. , vol.25 , pp. 160-165
    • Wawire, M.1    Oey, I.2    Mathooko, F.M.3    Njoroge, C.K.4    Shitanda, D.5    Sila, D.6    Hendrickx, M.7
  • 3
    • 67650392127 scopus 로고    scopus 로고
    • Sustainable Agriculture Network, Beltsville, MD, A. Clark (Ed.)
    • Managing Cover Crops Profitably: Cowpeas 2007, Sustainable Agriculture Network, Beltsville, MD. 3rd ed. A. Clark (Ed.).
    • (2007) Managing Cover Crops Profitably: Cowpeas
  • 4
    • 4143108012 scopus 로고    scopus 로고
    • Drought-induced effects and recovery of nitrate assimilation and nodule activity in cowpea plants inoculated with Bradyrhizobium spp. under moderate nitrate level
    • Silveira J.A.G., Costa R.C.L., Oliveira J.T.A. Drought-induced effects and recovery of nitrate assimilation and nodule activity in cowpea plants inoculated with Bradyrhizobium spp. under moderate nitrate level. Braz. J. Microbiol. 2001, 32:187-194.
    • (2001) Braz. J. Microbiol. , vol.32 , pp. 187-194
    • Silveira, J.A.G.1    Costa, R.C.L.2    Oliveira, J.T.A.3
  • 5
    • 58649092392 scopus 로고    scopus 로고
    • The major economic field diseases of cowpea in the humid agro-ecologies of South-western Nigeria
    • Adegbite A.A., Amusa N.A. The major economic field diseases of cowpea in the humid agro-ecologies of South-western Nigeria. Afr. J. Biotechnol. 2008, 7:4706-4712.
    • (2008) Afr. J. Biotechnol. , vol.7 , pp. 4706-4712
    • Adegbite, A.A.1    Amusa, N.A.2
  • 6
    • 80054866664 scopus 로고    scopus 로고
    • Recent advances in cowpea [Vigna unguiculata (L.) Walp.] omics research for genetic improvement
    • Diouf D. Recent advances in cowpea [Vigna unguiculata (L.) Walp.] omics research for genetic improvement. Afr. J. Biotechnol. 2011, 10:2803-2810.
    • (2011) Afr. J. Biotechnol. , vol.10 , pp. 2803-2810
    • Diouf, D.1
  • 8
    • 79251594440 scopus 로고    scopus 로고
    • Inducing fungus-resistance into plants through biotechnology
    • Wani S.H. Inducing fungus-resistance into plants through biotechnology. Not. Sci. Biol. 2010, 2:14-21.
    • (2010) Not. Sci. Biol. , vol.2 , pp. 14-21
    • Wani, S.H.1
  • 9
    • 84859234253 scopus 로고    scopus 로고
    • Proteomics and plant disease: advances in combating a major threat to the global food supply
    • Rampitsch C., Bykova N.V. Proteomics and plant disease: advances in combating a major threat to the global food supply. Proteomics 2012, 12:673-690.
    • (2012) Proteomics , vol.12 , pp. 673-690
    • Rampitsch, C.1    Bykova, N.V.2
  • 11
    • 84856655495 scopus 로고    scopus 로고
    • Proteomic identification of differentially expressed proteins in Gossypium thurberi inoculated with cotton Verticillium dahliae
    • Zhao F., Fang W., Xie D., Zhao Y., Tang Z., Li W., Nie L., Lv S. Proteomic identification of differentially expressed proteins in Gossypium thurberi inoculated with cotton Verticillium dahliae. Plant Sci. 2012, 185-186:176-184.
    • (2012) Plant Sci. , vol.185-186 , pp. 176-184
    • Zhao, F.1    Fang, W.2    Xie, D.3    Zhao, Y.4    Tang, Z.5    Li, W.6    Nie, L.7    Lv, S.8
  • 12
    • 84876742530 scopus 로고    scopus 로고
    • Comparative proteomic profiling in compatible and incompatible interactions between hop roots and Verticillium albo-atrum
    • Mandelc S., Timperman I., Radisek S., Devreese B., Samyn B., Javornik B. Comparative proteomic profiling in compatible and incompatible interactions between hop roots and Verticillium albo-atrum. Plant Physiol. Biochem. 2013, 68:23-31.
    • (2013) Plant Physiol. Biochem. , vol.68 , pp. 23-31
    • Mandelc, S.1    Timperman, I.2    Radisek, S.3    Devreese, B.4    Samyn, B.5    Javornik, B.6
  • 14
    • 33845290242 scopus 로고    scopus 로고
    • An efficient protein preparation for proteomic analysis of developing cotton fibers by 2-DE
    • Yao Y., Yang Y.-W., Liu J.-Y. An efficient protein preparation for proteomic analysis of developing cotton fibers by 2-DE. Electrophoresis 2006, 27:4559-4569.
    • (2006) Electrophoresis , vol.27 , pp. 4559-4569
    • Yao, Y.1    Yang, Y.-W.2    Liu, J.-Y.3
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 3543031771 scopus 로고
    • Elicitation of defense responses in bean leaves by Botrytis cinerea polygalacturonase
    • Urbanek H., Kuzniak-Gebarowska E., Herka K. Elicitation of defense responses in bean leaves by Botrytis cinerea polygalacturonase. Acta Physiol. Plant. 1991, 13:43-50.
    • (1991) Acta Physiol. Plant. , vol.13 , pp. 43-50
    • Urbanek, H.1    Kuzniak-Gebarowska, E.2    Herka, K.3
  • 19
    • 78651153791 scopus 로고
    • Disk electrophoresis. II. Method and application to human serum proteins
    • Davis B.J. Disk electrophoresis. II. Method and application to human serum proteins. Ann. Rev. N. Y. Acad. Sci. 1964, 121:404-427.
    • (1964) Ann. Rev. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 20
    • 78651163419 scopus 로고
    • Disk electrophoresis. I. Background and theory
    • Ornstein L. Disk electrophoresis. I. Background and theory. Ann. Rev. N. Y. Acad. Sci. 1964, 121:321-349.
    • (1964) Ann. Rev. N. Y. Acad. Sci. , vol.121 , pp. 321-349
    • Ornstein, L.1
  • 22
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel J., Asselin A. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 1989, 178:362-366.
    • (1989) Anal. Biochem. , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 23
    • 7244257594 scopus 로고    scopus 로고
    • PerlPrimer: cross-platform, graphical primer design for standard, bisulphite and real-time PCR
    • Marshall O.J. PerlPrimer: cross-platform, graphical primer design for standard, bisulphite and real-time PCR. Bioinformatics 2004, 20:2471-2472.
    • (2004) Bioinformatics , vol.20 , pp. 2471-2472
    • Marshall, O.J.1
  • 25
    • 45449087921 scopus 로고    scopus 로고
    • QBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data
    • Hellemans J., Mortier G., De Paepe A., Speleman F., Vandesompele J. qBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data. Genome Biol. 2007, 8:R19.
    • (2007) Genome Biol. , vol.8
    • Hellemans, J.1    Mortier, G.2    De Paepe, A.3    Speleman, F.4    Vandesompele, J.5
  • 26
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • research 0034.1-0034.11
    • Vandesompele J., De Preter K., Pattyn F., Poppe B., Van Roy N., De Paepe A., Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 2002, 3. research 0034.1-0034.11.
    • (2002) Genome Biol. , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 27
    • 19444381863 scopus 로고    scopus 로고
    • Reactive oxygen species generation and peroxidase activity during Oidium neolycopersici infection on Lycopersicon species
    • Mlícková K., Luhová L., Lebeda A., Mieslerová B., Pec P. Reactive oxygen species generation and peroxidase activity during Oidium neolycopersici infection on Lycopersicon species. Plant Physiol. Biochem. 2004, 42:753-761.
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 753-761
    • Mlícková, K.1    Luhová, L.2    Lebeda, A.3    Mieslerová, B.4    Pec, P.5
  • 28
    • 0033543516 scopus 로고    scopus 로고
    • Hydroperoxide assay with the ferric-xylenol orange complex
    • Gay C., Collins J., Gebicki J.M. Hydroperoxide assay with the ferric-xylenol orange complex. Anal. Biochem. 1999, 273:149-155.
    • (1999) Anal. Biochem. , vol.273 , pp. 149-155
    • Gay, C.1    Collins, J.2    Gebicki, J.M.3
  • 32
    • 33646562521 scopus 로고    scopus 로고
    • Metabolic consequences of susceptibility and resistance in barley leaves challenged with powdery mildew
    • Swarbrick P.J., Schulze-Lefert P., Scholes J.D. Metabolic consequences of susceptibility and resistance in barley leaves challenged with powdery mildew. Plant Cell Environ. 2006, 29:1061-1076.
    • (2006) Plant Cell Environ. , vol.29 , pp. 1061-1076
    • Swarbrick, P.J.1    Schulze-Lefert, P.2    Scholes, J.D.3
  • 33
    • 40049096921 scopus 로고    scopus 로고
    • Plant physiology meets phytopathology: plant primary metabolism and plant-pathogen interactions
    • Berger S., Sinha A.K., Roitsch T. Plant physiology meets phytopathology: plant primary metabolism and plant-pathogen interactions. J. Exp. Bot. 2007, 58:4019-4026.
    • (2007) J. Exp. Bot. , vol.58 , pp. 4019-4026
    • Berger, S.1    Sinha, A.K.2    Roitsch, T.3
  • 34
    • 0032422614 scopus 로고    scopus 로고
    • Plant NADP-dependent isocitrate dehydrogenases are predominantly localized in the cytosol
    • Chen R. Plant NADP-dependent isocitrate dehydrogenases are predominantly localized in the cytosol. Planta 1998, 207:280-285.
    • (1998) Planta , vol.207 , pp. 280-285
    • Chen, R.1
  • 36
    • 51549114743 scopus 로고    scopus 로고
    • RNAi-mediated repression of cell wall invertase impairs defense in source leaves of tobacco
    • Essmann J., Schmitz-Thom I., Schon H., Sonnewald S., Weis E., Scharte J. RNAi-mediated repression of cell wall invertase impairs defense in source leaves of tobacco. Plant Physiol. 2008, 47:1288-1299.
    • (2008) Plant Physiol. , vol.47 , pp. 1288-1299
    • Essmann, J.1    Schmitz-Thom, I.2    Schon, H.3    Sonnewald, S.4    Weis, E.5    Scharte, J.6
  • 37
    • 77952240149 scopus 로고    scopus 로고
    • Photosynthetic and respiratory changes in leaves of poplar elicited by rust infection
    • Major I.T., Nicole M-C., Duplessis S., Séguin A. Photosynthetic and respiratory changes in leaves of poplar elicited by rust infection. Photosynth. Res. 2010, 104:41-48.
    • (2010) Photosynth. Res. , vol.104 , pp. 41-48
    • Major, I.T.1    Nicole, M.-C.2    Duplessis, S.3    Séguin, A.4
  • 39
    • 67651049051 scopus 로고    scopus 로고
    • Photorespiratory metabolism: genes, mutants, energetics, and redox signaling
    • Foyer C.H., Bloom A.J., Queval G., Noctor G. Photorespiratory metabolism: genes, mutants, energetics, and redox signaling. Annu. Rev. Plant Biol. 2009, 60:455-484.
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 455-484
    • Foyer, C.H.1    Bloom, A.J.2    Queval, G.3    Noctor, G.4
  • 40
    • 84863797323 scopus 로고    scopus 로고
    • 2 production during plant defense responses and functions independently from NADPH oxidase
    • 2 production during plant defense responses and functions independently from NADPH oxidase. Plant Signal. Behav. 2012, 7:752-755.
    • (2012) Plant Signal. Behav. , vol.7 , pp. 752-755
    • Rojas, C.M.1    Mysore, K.S.2
  • 41
    • 0036593051 scopus 로고    scopus 로고
    • Drought and oxidative load in the leaves of the C3 plants: a predominant role for photorespiration?
    • Noctor G., Veljovic-Jovanovic S., Driscoll S., Novitskaya L., Foyer C.H. Drought and oxidative load in the leaves of the C3 plants: a predominant role for photorespiration?. Ann. Bot. 2002, 89:841-850.
    • (2002) Ann. Bot. , vol.89 , pp. 841-850
    • Noctor, G.1    Veljovic-Jovanovic, S.2    Driscoll, S.3    Novitskaya, L.4    Foyer, C.H.5
  • 42
    • 84863230574 scopus 로고    scopus 로고
    • Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis
    • Rojas C.M., Senthil-Kumar M., Wang K., Ryu C.M., Kaunda L.A., Mysore K.S. Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis. Plant Cell 2012, 24:336-352.
    • (2012) Plant Cell , vol.24 , pp. 336-352
    • Rojas, C.M.1    Senthil-Kumar, M.2    Wang, K.3    Ryu, C.M.4    Kaunda, L.A.5    Mysore, K.S.6
  • 44
    • 1942501872 scopus 로고    scopus 로고
    • The Arabidopsis cyclophilin gene family 1
    • Romano P.G.N., Horton P., Gray J.E. The Arabidopsis cyclophilin gene family 1. Plant Physiol. 2004, 134:1268-1282.
    • (2004) Plant Physiol. , vol.134 , pp. 1268-1282
    • Romano, P.G.N.1    Horton, P.2    Gray, J.E.3
  • 45
    • 17644371362 scopus 로고    scopus 로고
    • Activation of a phytopathogenetic bacteria effector protein by eukaryotic cyclophilins
    • Coaker G., Falik A., Staskawicz B. Activation of a phytopathogenetic bacteria effector protein by eukaryotic cyclophilins. Science 2005, 308:548-550.
    • (2005) Science , vol.308 , pp. 548-550
    • Coaker, G.1    Falik, A.2    Staskawicz, B.3
  • 46
    • 67349135788 scopus 로고    scopus 로고
    • Over-expression of aspartate aminotransferase genes in rice resulted in altered nitrogen metabolism and increased amino acid content in seeds
    • Zhou Y., Cai H., Xiao J., Li X., Zhang Q., Lian X. Over-expression of aspartate aminotransferase genes in rice resulted in altered nitrogen metabolism and increased amino acid content in seeds. Theor. Appl. Genet. 2009, 118:1381-1390.
    • (2009) Theor. Appl. Genet. , vol.118 , pp. 1381-1390
    • Zhou, Y.1    Cai, H.2    Xiao, J.3    Li, X.4    Zhang, Q.5    Lian, X.6
  • 47
    • 84867092052 scopus 로고    scopus 로고
    • Different roles of glycine-rich RNA-binding protein 7 in plant defense against Pectobacterium carotovorum, Botrytis cinerea, and tobacco mosaic viruses
    • Lee H.J., Kim J.S., Yoo S.J., Kang E.Y., Han S.H., Yang K.Y., Kim Y.C., et al. Different roles of glycine-rich RNA-binding protein 7 in plant defense against Pectobacterium carotovorum, Botrytis cinerea, and tobacco mosaic viruses. Plant Physiol. Biochem. 2012, 60:46-52.
    • (2012) Plant Physiol. Biochem. , vol.60 , pp. 46-52
    • Lee, H.J.1    Kim, J.S.2    Yoo, S.J.3    Kang, E.Y.4    Han, S.H.5    Yang, K.Y.6    Kim, Y.C.7
  • 50
    • 84881437199 scopus 로고    scopus 로고
    • A translationally controlled tumor protein negatively regulates the hypersensitive response in Nicotiana benthamiana
    • Gupta M., Yoshioka H., Ohnishi K., Mizumoto H., Hikichi Y., Kiba A. A translationally controlled tumor protein negatively regulates the hypersensitive response in Nicotiana benthamiana. Plant Cell Physiol. 2013, 1-12.
    • (2013) Plant Cell Physiol. , pp. 1-12
    • Gupta, M.1    Yoshioka, H.2    Ohnishi, K.3    Mizumoto, H.4    Hikichi, Y.5    Kiba, A.6
  • 51
    • 84878891130 scopus 로고    scopus 로고
    • ZmLEA3, a multifunctional group 3 LEA protein from maize (Zea mays L.) is involved in biotic and abiotic stresses
    • Liu Y., Wang L., Xing X., Sun L., Pan J., Kong X., Zhang M., Li D. ZmLEA3, a multifunctional group 3 LEA protein from maize (Zea mays L.) is involved in biotic and abiotic stresses. Plant Cell Physiol. 2013, 54:944-959.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 944-959
    • Liu, Y.1    Wang, L.2    Xing, X.3    Sun, L.4    Pan, J.5    Kong, X.6    Zhang, M.7    Li, D.8
  • 52
    • 0024418447 scopus 로고    scopus 로고
    • Stress proteins, infection and immune surveillance
    • Young R.A., Elliott T.J. Stress proteins, infection and immune surveillance. Cell 2002, 59:5-8.
    • (2002) Cell , vol.59 , pp. 5-8
    • Young, R.A.1    Elliott, T.J.2
  • 54
    • 78650988662 scopus 로고    scopus 로고
    • Ascorbate and glutathione. The heart of the redox hub
    • Foyer C.H., Noctor G. Ascorbate and glutathione. The heart of the redox hub. Plant Physiol. 2011, 155:2-18.
    • (2011) Plant Physiol. , vol.155 , pp. 2-18
    • Foyer, C.H.1    Noctor, G.2
  • 55
  • 56
    • 84874768482 scopus 로고    scopus 로고
    • 2-induced leaf cell death and the crosstalk of reactive nitric/oxygen species
    • 2-induced leaf cell death and the crosstalk of reactive nitric/oxygen species. J. Integr. Plant Biol. 2013, 55:202-208.
    • (2013) J. Integr. Plant Biol. , vol.55 , pp. 202-208
    • Wang, Y.1    Lin, A.2    Loake, G.J.3
  • 58
    • 33750996449 scopus 로고    scopus 로고
    • Hydrogen peroxide, nitric oxide and cytosolic ascorbate peroxidase at the crossroad between defence and cell death
    • de Pinto M.C., Paradiso A., Leonetti P., de Gara L. Hydrogen peroxide, nitric oxide and cytosolic ascorbate peroxidase at the crossroad between defence and cell death. Plant J. 2006, 48:784-795.
    • (2006) Plant J. , vol.48 , pp. 784-795
    • de Pinto, M.C.1    Paradiso, A.2    Leonetti, P.3    de Gara, L.4
  • 59
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • Van Loon L.C., Rep M., Pieterse C.M.J. Significance of inducible defense-related proteins in infected plants. Annu. Rev. Phytopathol. 2006, 44:135-162.
    • (2006) Annu. Rev. Phytopathol. , vol.44 , pp. 135-162
    • Van Loon, L.C.1    Rep, M.2    Pieterse, C.M.J.3
  • 60
    • 0029787094 scopus 로고    scopus 로고
    • The major birch pollen allergen, Bet v 1, shows ribonuclease activity
    • Bufe A., Spangfort M.D., Kahlert H., Schlaak M., Becker W.-M. The major birch pollen allergen, Bet v 1, shows ribonuclease activity. Planta 1996, 199:413-415.
    • (1996) Planta , vol.199 , pp. 413-415
    • Bufe, A.1    Spangfort, M.D.2    Kahlert, H.3    Schlaak, M.4    Becker, W.-M.5
  • 61
    • 33750359717 scopus 로고    scopus 로고
    • The family 10 of plant pathogenesis-related proteins: their structure, regulation, and function in response to biotic and abiotic stresses
    • Liu J-J., Ekramoddoullah A.K.M. The family 10 of plant pathogenesis-related proteins: their structure, regulation, and function in response to biotic and abiotic stresses. Physiol. Mol. Plant Pathol. 2006, 68:3-13.
    • (2006) Physiol. Mol. Plant Pathol. , vol.68 , pp. 3-13
    • Liu, J.-J.1    Ekramoddoullah, A.K.M.2
  • 62
    • 3042810007 scopus 로고    scopus 로고
    • The plant proteolytic machinery and its role in defense
    • Vander Hoorn R.A., Jones J.D. The plant proteolytic machinery and its role in defense. Curr. Opin. Plant Biol. 2004, 7:400-407.
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 400-407
    • Vander Hoorn, R.A.1    Jones, J.D.2
  • 63
    • 0032534468 scopus 로고    scopus 로고
    • Activation of cysteine proteases in cowpea plants during the hypersensitive response - a form of programmed cell death
    • D'silva I., Poirier G.G., Heath M.C. Activation of cysteine proteases in cowpea plants during the hypersensitive response - a form of programmed cell death. Exp. Cell Res. 1998, 245:389-399.
    • (1998) Exp. Cell Res. , vol.245 , pp. 389-399
    • D'silva, I.1    Poirier, G.G.2    Heath, M.C.3
  • 64
    • 38949178970 scopus 로고    scopus 로고
    • Biochemical approaches for discovering protein-protein interactions
    • Miernyk J.A., Thelen J. Biochemical approaches for discovering protein-protein interactions. Plant J. 2008, 53:597-609.
    • (2008) Plant J. , vol.53 , pp. 597-609
    • Miernyk, J.A.1    Thelen, J.2


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