메뉴 건너뛰기




Volumn 46, Issue 6, 2005, Pages 1007-1015

A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress

Author keywords

Antifungal protein; Gentiana triflora; Peroxiredoxin Q; Recombinant protein; Thioredoxin peroxidase; Transgenic tobacco

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; CRASSULACEAE; FUNGI; GENTIANA; GENTIANA TRIFLORA; GENTIANACEAE; NICOTIANA OBTUSIFOLIA; NICOTIANA TABACUM; POPULUS BALSAMIFERA; SEDUM LINEARE; SUAEDA MARITIMA;

EID: 24644445236     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pci109     Document Type: Article
Times cited : (56)

References (38)
  • 2
    • 0033015532 scopus 로고    scopus 로고
    • Resistance to Botrytis cinerea in scented geranium transformed with a gene encoding the antimicrobial protein Ace-AMP1
    • Bi, Y.M., Vammue, B.P.A., Goodwin, P.H., KrishnaRaj, S. and Saxena, P.K. (1999) Resistance to Botrytis cinerea in scented geranium transformed with a gene encoding the antimicrobial protein Ace-AMP1. Plant Cell Reports 18: 835-840.
    • (1999) Plant Cell Reports , vol.18 , pp. 835-840
    • Bi, Y.M.1    Vammue, B.P.A.2    Goodwin, P.H.3    KrishnaRaj, S.4    Saxena, P.K.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and 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
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert, W.F., Terras, F.R.G., Cammue, B.P.A. and Osborn, R.W. (1995) Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. 108: 1353-1358.
    • (1995) Plant Physiol. , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 9
    • 0344177528 scopus 로고    scopus 로고
    • Plants ectopically expressing the iron-binding protein, ferritin, are tolerant to oxidative damage and pathogens
    • Deak, M., Horvath, G.V., Davletova, S., Torok, K., Sass, L., Vass, I., Barna, B., Kiraly, Z. and Dudits, D. (1999) Plants ectopically expressing the iron-binding protein, ferritin, are tolerant to oxidative damage and pathogens. Nature Biotechnol. 17: 192-196.
    • (1999) Nature Biotechnol. , vol.17 , pp. 192-196
    • Deak, M.1    Horvath, G.V.2    Davletova, S.3    Torok, K.4    Sass, L.5    Vass, I.6    Barna, B.7    Kiraly, Z.8    Dudits, D.9
  • 10
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • Dietz, K.J., Horling, F., Konig, J. and Baier, M. (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J. Exp. Bot. 53: 1321-1329.
    • (2002) J. Exp. Bot. , vol.53 , pp. 1321-1329
    • Dietz, K.J.1    Horling, F.2    Konig, J.3    Baier, M.4
  • 11
    • 0031128435 scopus 로고    scopus 로고
    • Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum
    • Epple, P., Apel, K. and Bohlman, H. (1997) Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum. Plant Cell 9: 509-520.
    • (1997) Plant Cell , vol.9 , pp. 509-520
    • Epple, P.1    Apel, K.2    Bohlman, H.3
  • 12
    • 0031743859 scopus 로고    scopus 로고
    • Transgenic approaches to disease protection: Applications of antifungal proteins
    • Evans, I.J. and Greenland, A.J. (1998) Transgenic approaches to disease protection: applications of antifungal proteins. Pesticide Sci. 54: 353-359.
    • (1998) Pesticide Sci. , vol.54 , pp. 353-359
    • Evans, I.J.1    Greenland, A.J.2
  • 13
    • 0028518533 scopus 로고
    • Thionines: Properties, possible biological roles and mechanisms of action
    • Florack, D.E.A. and Stiekema, W.J. (1994) Thionines: properties, possible biological roles and mechanisms of action. Plant Mol. Biol. 26: 25-37.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 25-37
    • Florack, D.E.A.1    Stiekema, W.J.2
  • 14
    • 0025933319 scopus 로고
    • Pathogenesis-related protein 4 is structurally homologous to the carboxy-terminal domains of hevein, Win-1 and Win-2
    • Friedrich, L., Moyer, M., Ward, E. and Ryals, J. (1991) Pathogenesis-related protein 4 is structurally homologous to the carboxy-terminal domains of hevein, Win-1 and Win-2. Mol. Gen. Genet. 230: 113-119.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 113-119
    • Friedrich, L.1    Moyer, M.2    Ward, E.3    Ryals, J.4
  • 15
    • 0028833949 scopus 로고
    • The defensive role of non specific lipid-transfer proteins in plants
    • Garcia-Olmedo, F., Molina, A., Segura, A. and Mooreno, M. (1995) The defensive role of non specific lipid-transfer proteins in plants. Trends Microbiol. 3: 72-75.
    • (1995) Trends Microbiol. , vol.3 , pp. 72-75
    • Garcia-Olmedo, F.1    Molina, A.2    Segura, A.3    Mooreno, M.4
  • 16
    • 0034729657 scopus 로고    scopus 로고
    • The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea
    • Govrin, E.M. and Levine, A. (2000) The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea. Curr. Biol. 10: 751-757.
    • (2000) Curr. Biol. , vol.10 , pp. 751-757
    • Govrin, E.M.1    Levine, A.2
  • 17
    • 0034031475 scopus 로고    scopus 로고
    • Activation of a diverse set of genes during the tobacco resistance response to TMV is independent of salicylic acid; induction of a subset is also ethylene independent
    • Guo, A., Salih G. and Klessig, D.F. (2000) Activation of a diverse set of genes during the tobacco resistance response to TMV is independent of salicylic acid; induction of a subset is also ethylene independent. Plant J. 21: 409-418.
    • (2000) Plant J. , vol.21 , pp. 409-418
    • Guo, A.1    Salih, G.2    Klessig, D.F.3
  • 18
    • 0026633092 scopus 로고
    • Antifungal activity of chitin-binding proteins from barley grain and stressed leaf
    • Hejgaard, J., Jacobsen, S., Bjorn, S.E. and Kragh, K.M. (1992) Antifungal activity of chitin-binding proteins from barley grain and stressed leaf. FEBS Lett. 307: 389-392.
    • (1992) FEBS Lett. , vol.307 , pp. 389-392
    • Hejgaard, J.1    Jacobsen, S.2    Bjorn, S.E.3    Kragh, K.M.4
  • 19
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • Horling, F., Lamkemeyer, P., Konig, J., Finkemeier, I., Kandlbinder, A., Baier, M. and Dietz, K.J. (2003) Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol. 131: 317-325.
    • (2003) Plant Physiol. , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    Konig, J.3    Finkemeier, I.4    Kandlbinder, A.5    Baier, M.6    Dietz, K.J.7
  • 21
    • 0037361851 scopus 로고    scopus 로고
    • C-terminal domain of a hevein-like protein from Wasabia japonica has potent anti-microbial activity
    • Kiba, A., Saitoh, H., Nishihara, M., Omiya, K. and Yamamura, S. (2003) C-terminal domain of a hevein-like protein from Wasabia japonica has potent anti-microbial activity. Plant Cell Physiol. 44: 296-303.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 296-303
    • Kiba, A.1    Saitoh, H.2    Nishihara, M.3    Omiya, K.4    Yamamura, S.5
  • 22
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • Kong, W., Shiota, S., Shi, Y., Nakayama, H. and Nakayama, K. (2000) A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem. J. 351: 107-114.
    • (2000) Biochem. J. , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 15: 680-685.
    • (1970) Nature , vol.15 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 33644535944 scopus 로고
    • Pathogenesis-related proteins of plants
    • Linthorst, H.J.M. (1991) Pathogenesis-related proteins of plants. Crit. Rev. Plant Sci. 10: 123-150.
    • (1991) Crit. Rev. Plant Sci. , vol.10 , pp. 123-150
    • Linthorst, H.J.M.1
  • 25
    • 0031239810 scopus 로고    scopus 로고
    • Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2
    • Molina, A. and Garcia-Olmedo, F. (1997) Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2. Plant J. 12: 669-675.
    • (1997) Plant J. , vol.12 , pp. 669-675
    • Molina, A.1    Garcia-Olmedo, F.2
  • 26
    • 0034724503 scopus 로고    scopus 로고
    • Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4, 504, 864 bp covered by sixty P1 and TAC clones
    • Nakamura, Y. (2000) Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4, 504, 864 bp covered by sixty P1 and TAC clones. DNA Res. 7: 131-135.
    • (2000) DNA Res. , vol.7 , pp. 131-135
    • Nakamura, Y.1
  • 27
    • 0031801556 scopus 로고    scopus 로고
    • Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves
    • Niki, T., Mitsuhara, I., Seo, S., Ohtsubo, N. and Ohashi, Y. (1998) Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves. Plant Cell Physiol. 39: 500-507.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 500-507
    • Niki, T.1    Mitsuhara, I.2    Seo, S.3    Ohtsubo, N.4    Ohashi, Y.5
  • 28
    • 0000116053 scopus 로고
    • Stress-induced expression of gene for pathogenesis-related proteins in plants
    • Ohashi, Y. and Ohshima, M. (1992) Stress-induced expression of gene for pathogenesis-related proteins in plants. Plant Cell Physiol. 33: 819-826.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 819-826
    • Ohashi, Y.1    Ohshima, M.2
  • 31
    • 0028029709 scopus 로고
    • Protection from oxidative stress in transgenic plants
    • Rennenberg, H. and Polle, A. (1994) Protection from oxidative stress in transgenic plants. Biochem. Soc. Trans 22: 936-940.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 936-940
    • Rennenberg, H.1    Polle, A.2
  • 34
    • 0036342422 scopus 로고    scopus 로고
    • Overexpression of glutathione S-transferase in transgenic rice enhances germination and growth at low temperature
    • Takesawa, T., Ito, M., Kanzaki, H., Kameya, N. and Nakamura, I. (2002) Overexpression of glutathione S-transferase in transgenic rice enhances germination and growth at low temperature. Mol. Breed. 9: 93-101
    • (2002) Mol. Breed. , vol.9 , pp. 93-101
    • Takesawa, T.1    Ito, M.2    Kanzaki, H.3    Kameya, N.4    Nakamura, I.5
  • 35
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene, regulation, and cellular function in animals, plants and microorganisms
    • Theil, E.C. (1987) Ferritin: structure, gene, regulation, and cellular function in animals, plants and microorganisms. Annu. Rev. Biochem. 56: 289-315.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 38
    • 0030041342 scopus 로고    scopus 로고
    • Analysis of late-blight disease resistance and freezing tolerance in transgenic potato plants expressing sense and antisense genes for an osmotin-like protein
    • Zhu, B., Chen, T.H.H. and Li, P.H. (1996) Analysis of late-blight disease resistance and freezing tolerance in transgenic potato plants expressing sense and antisense genes for an osmotin-like protein. Planta 198: 70-77.
    • (1996) Planta , vol.198 , pp. 70-77
    • Zhu, B.1    Chen, T.H.H.2    Li, P.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.