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Volumn 33, Issue 5, 1997, Pages 887-895

The consequence of peroxidase overexpression in transgenic plants on root growth and development

Author keywords

auxin; indoleacetic acid; Nicotiana sylvestris; Nicotiana tabacum; root growth; tobacco peroxidase; transgenic plants

Indexed keywords

INDOLEACETIC ACID; INDOLEACETIC ACID DERIVATIVE; ISOENZYME; PEROXIDASE; PHYTOHORMONE; RECOMBINANT PROTEIN; TOBACCO ANIONIC PEROXIDASE; WATER;

EID: 0031105538     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005756713493     Document Type: Article
Times cited : (83)

References (28)
  • 1
    • 0005532594 scopus 로고
    • Relationships between peroxidatic activities and cell wall plasticity
    • Greppin H, Penel C, Gaspar T (eds) University of Geneva Press, Geneva, Switzerland
    • Goldberg R, Imberty A, Liberman M, Prat R: Relationships between peroxidatic activities and cell wall plasticity. In: Greppin H, Penel C, Gaspar T (eds) Molecular and Physiological Aspects of Plant Peroxidases, pp. 208-220. University of Geneva Press, Geneva, Switzerland (1986).
    • (1986) Molecular and Physiological Aspects of Plant Peroxidases , pp. 208-220
    • Goldberg, R.1    Imberty, A.2    Liberman, M.3    Prat, R.4
  • 2
    • 34250144281 scopus 로고
    • The relationship between oxidase activity, peroxidase activity, hydrogen peroxidase, and phenolic compounds in the degradation of indole-3-acetic acid in vitro
    • Grambow HJ, Langenbeck-Schwich B: The relationship between oxidase activity, peroxidase activity, hydrogen peroxidase, and phenolic compounds in the degradation of indole-3-acetic acid in vitro. Planta 157: 131-137 (1983).
    • (1983) Planta , vol.157 , pp. 131-137
    • Grambow, H.J.1    Langenbeck-Schwich, B.2
  • 3
    • 0001715184 scopus 로고
    • Role of peroxidase in lignification of tobacco cells
    • Mäder M, Füssl R: Role of peroxidase in lignification of tobacco cells. Plant Physiol 70: 1132-1134 (1982).
    • (1982) Plant Physiol , vol.70 , pp. 1132-1134
    • Mäder, M.1    Füssl, R.2
  • 4
    • 0000493904 scopus 로고
    • Lignins
    • Conn E. Academic Press, New York
    • Grisebach H: Lignins. In: Conn E. The Biochemistry of Plants, Vol 7, pp. 457-478. Academic Press, New York (1981).
    • (1981) The Biochemistry of Plants , vol.7 , pp. 457-478
    • Grisebach, H.1
  • 5
    • 11544297023 scopus 로고
    • Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase
    • Lagrimini LM: Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase. Plant Physiol 96: 577-583 (1991).
    • (1991) Plant Physiol , vol.96 , pp. 577-583
    • Lagrimini, L.M.1
  • 6
    • 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: Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue. Plant Physiol 81: 487-492 (1986).
    • (1986) Plant Physiol , vol.81 , pp. 487-492
    • Espelie, K.E.1    Franceschi, V.R.2    Kolattukudy, P.E.3
  • 7
    • 0027028408 scopus 로고
    • Phenolic compounds and their role in disease resistance
    • Nicholson RL, Hammerschmidt R: Phenolic compounds and their role in disease resistance. Annu Rev Phytopath 30: 369-389 (1992).
    • (1992) Annu Rev Phytopath , vol.30 , pp. 369-389
    • Nicholson, R.L.1    Hammerschmidt, R.2
  • 8
    • 0000651861 scopus 로고
    • Peroxidase over-production in tomato: Wound-induced polyphenol deposition and disease resistance
    • Lagrimini LM, Vaughn J, Erb WA, Miller SA: Peroxidase over-production in tomato: wound-induced polyphenol deposition and disease resistance. HortScience 28: 218-221 (1993).
    • (1993) HortScience , vol.28 , pp. 218-221
    • Lagrimini, L.M.1    Vaughn, J.2    Erb, W.A.3    Miller, S.A.4
  • 9
    • 0001778765 scopus 로고
    • Plant peroxidases: Structure-function relationships
    • Penel C, Gaspar T, Greppin H (eds) University of Geneva, Geneva, Switzerland
    • Welinder KG: Plant peroxidases: structure-function relationships. In: Penel C, Gaspar T, Greppin H (eds) Plant Peroxidases 1980-1990, pp. 1-24. University of Geneva, Geneva, Switzerland (1992).
    • (1992) Plant Peroxidases 1980-1990 , pp. 1-24
    • Welinder, K.G.1
  • 10
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • Everse J, Everse KE, Grisham M (eds) CRC Press, Boca Raton, FL
    • Dunford HB: Horseradish peroxidase: structure and kinetic properties. In: Everse J, Everse KE, Grisham M (eds) Peroxidases in Chemistry and Biology, pp. 1-24. CRC Press, Boca Raton, FL (1991).
    • (1991) Peroxidases in Chemistry and Biology , pp. 1-24
    • Dunford, H.B.1
  • 11
    • 0030111427 scopus 로고    scopus 로고
    • Tobacco anionic peroxidase overexpressed in transgenic plants. I. Purification and unusual kinetic properties
    • Gazaryan IG, Lagrimini LM: Tobacco anionic peroxidase overexpressed in transgenic plants. I. Purification and unusual kinetic properties. Phytochemistry 41: 1029-1034 (1996).
    • (1996) Phytochemistry , vol.41 , pp. 1029-1034
    • Gazaryan, I.G.1    Lagrimini, L.M.2
  • 12
    • 0000435925 scopus 로고
    • Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection
    • Lagrimini LM, Rothstein S: Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection. Plant Physiol 84: 438-442 (1987).
    • (1987) Plant Physiol , vol.84 , pp. 438-442
    • Lagrimini, L.M.1    Rothstein, S.2
  • 13
    • 0001490428 scopus 로고
    • On the physiological significance of the isoenzyme groups of peroxidase from tobacco demonstrated by biochemical properties. II. pH-optima, michaelis-constants, maximal oxidation-rates
    • Mäder M, Nessel N, Bopp M: On the physiological significance of the isoenzyme groups of peroxidase from tobacco demonstrated by biochemical properties. II. pH-optima, michaelis-constants, maximal oxidation-rates. Pflanzenphysiol 82: 247-260 (1977).
    • (1977) Pflanzenphysiol , vol.82 , pp. 247-260
    • Mäder, M.1    Nessel, N.2    Bopp, M.3
  • 14
    • 0842293228 scopus 로고
    • Altered phenotypes in plants transformed with chimeric tobacco peroxidase genes
    • Lobarzewski J, Greppin H, Penel C, Gaspar T (eds) University of Geneva, Geneva, Switzerland
    • Lagrimini LM: Altered phenotypes in plants transformed with chimeric tobacco peroxidase genes. In: Lobarzewski J, Greppin H, Penel C, Gaspar T (eds) Biochemical, Molecular and Physiological Aspects of Plant Peroxidases, pp. 59-67. University of Geneva, Geneva, Switzerland (1991).
    • (1991) Biochemical, Molecular and Physiological Aspects of Plant Peroxidases , pp. 59-67
    • Lagrimini, L.M.1
  • 15
    • 11944253488 scopus 로고
    • Peroxidase induced wilting in transgenic tobacco plants
    • Lagrimini LM, Bradford S, Rothstein S: Peroxidase induced wilting in transgenic tobacco plants. Plant Cell 2: 7-18 (1990).
    • (1990) Plant Cell , vol.2 , pp. 7-18
    • Lagrimini, L.M.1    Bradford, S.2    Rothstein, S.3
  • 17
    • 0000599951 scopus 로고
    • Effects of sodium chloride on the hydraulic conductivity of soybean root systems
    • Joly RJ: Effects of sodium chloride on the hydraulic conductivity of soybean root systems. Plant Physiol 91: 1262-1265 (1990).
    • (1990) Plant Physiol , vol.91 , pp. 1262-1265
    • Joly, R.J.1
  • 18
    • 0000195967 scopus 로고
    • A simple purification of indole-3-acetic acid and abscisic acid for GC-SIM-MS analysis by microfiltration of aqueous samples through nylon
    • Dunlap JR, Guinn G: A simple purification of indole-3-acetic acid and abscisic acid for GC-SIM-MS analysis by microfiltration of aqueous samples through nylon. Plant Physiol 90: 197-201 (1989).
    • (1989) Plant Physiol , vol.90 , pp. 197-201
    • Dunlap, J.R.1    Guinn, G.2
  • 20
    • 0030186876 scopus 로고    scopus 로고
    • Tobacco anionic peroxidase overexpressed in transgenic plants. II. Aerobic oxidation of indole-3-acetic acid
    • Gazaryan IG, Lagrimini LM: Tobacco anionic peroxidase overexpressed in transgenic plants. II. Aerobic oxidation of indole-3-acetic acid. Phytochemistry 42: 1271-1278 (1996).
    • (1996) Phytochemistry , vol.42 , pp. 1271-1278
    • Gazaryan, I.G.1    Lagrimini, L.M.2
  • 21
    • 0000355618 scopus 로고
    • On the inhibition of bud development and other functions of growth substances in Vicia faba
    • Thimann KV, Skoog F: On the inhibition of bud development and other functions of growth substances in Vicia faba. Proc R Soc B114: 317-339 (1934).
    • (1934) Proc R Soc , vol.B114 , pp. 317-339
    • Thimann, K.V.1    Skoog, F.2
  • 22
    • 0002760269 scopus 로고
    • Hormonal factors controlling the initiation and development of lateral roots
    • Wrightman F, Schneider E, Thinman KV: Hormonal factors controlling the initiation and development of lateral roots. Physiol Plant 49: 304-314 (1990).
    • (1990) Physiol Plant , vol.49 , pp. 304-314
    • Wrightman, F.1    Schneider, E.2    Thinman, K.V.3
  • 23
    • 0001623103 scopus 로고
    • Alterations of endogenous cytokinins in transgenic plants using a chimeric isopentenyl transferase gene
    • Medford JI, Morgan R, El-Sawi Z, Klee HK: Alterations of endogenous cytokinins in transgenic plants using a chimeric isopentenyl transferase gene. Plant Cell 1: 403-413 (1989).
    • (1989) Plant Cell , vol.1 , pp. 403-413
    • Medford, J.I.1    Morgan, R.2    El-Sawi, Z.3    Klee, H.K.4
  • 24
    • 0028675592 scopus 로고
    • Promoter tagging with a promoterless ipt gene leads to cytokinin-induced phenotypic variability in transgenic tobacco plants: Implications of gene dosage effects
    • Hewlett A, Prinsen E, Schell J, van Onckelen H, Schmülling T: Promoter tagging with a promoterless ipt gene leads to cytokinin-induced phenotypic variability in transgenic tobacco plants: Implications of gene dosage effects. Plant J 6: 879-891 (1994).
    • (1994) Plant J , vol.6 , pp. 879-891
    • Hewlett, A.1    Prinsen, E.2    Schell, J.3    Van Onckelen, H.4    Schmülling, T.5
  • 25
    • 0026092265 scopus 로고
    • Inactivation of auxin in tobacco transformed with the indoleacetic acid-lysine synthetase gene of Pseudomonas savastanoi
    • Romano CP, Hein MB, Klee HJ: Inactivation of auxin in tobacco transformed with the indoleacetic acid-lysine synthetase gene of Pseudomonas savastanoi. Genes Devel 5: 438-446 (1991).
    • (1991) Genes Devel , vol.5 , pp. 438-446
    • Romano, C.P.1    Hein, M.B.2    Klee, H.J.3
  • 26
    • 0001680050 scopus 로고
    • Transgenic tobacco plants coexpressing the Agrobacterium tumefaciens iaaM and iaaH genes display altered growth and indoleacetic acid metabolism
    • Sitbon F, Hennion S, Sundberg B, Little CHA, Olsson O, Sandberg G: Transgenic tobacco plants coexpressing the Agrobacterium tumefaciens iaaM and iaaH genes display altered growth and indoleacetic acid metabolism. Plant Physiol 99: 1062-1069 (1992).
    • (1992) Plant Physiol , vol.99 , pp. 1062-1069
    • Sitbon, F.1    Hennion, S.2    Sundberg, B.3    Little, C.H.A.4    Olsson, O.5    Sandberg, G.6
  • 27
    • 0000793141 scopus 로고
    • Peroxidase catalyzed oxidation of indole-3-acetic acid
    • Hinman RL, Lang L: Peroxidase catalyzed oxidation of indole-3-acetic acid. Biochemistry 4: 144-158 (1965).
    • (1965) Biochemistry , vol.4 , pp. 144-158
    • Hinman, R.L.1    Lang, L.2
  • 28
    • 0030031097 scopus 로고    scopus 로고
    • The mechanism of indole-3-acetic acid oxidation by plant peroxidases. Anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases
    • RNF
    • Gazaryan IG, Lagrimini LM, Ashby GA, RNF: The mechanism of indole-3-acetic acid oxidation by plant peroxidases. Anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases. Biochem J 313: 841-847 (1996).
    • (1996) Biochem J , vol.313 , pp. 841-847
    • Gazaryan, I.G.1    Lagrimini, L.M.2    Ashby, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.