메뉴 건너뛰기




Volumn 46, Issue 9, 2005, Pages 1540-1548

Molecular cloning and characterization of a senescence-induced tau-class glutathione S-transferase from barley leaves

Author keywords

Barley (Hordeum vulgare L.); Cloning; Glutathione S transferase; Senescence; Stress response

Indexed keywords

GLUTATHIONE TRANSFERASE; PLANT DNA;

EID: 26444560492     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pci167     Document Type: Article
Times cited : (25)

References (46)
  • 2
    • 1542543831 scopus 로고    scopus 로고
    • Abiotic stress alters transcript profiles and activity of glutathione S-transferase, glutathione peroxidase, and glutathione reductase in Euphorbia esula
    • Anderson, J.V. and Davis, D.G. (2004) Abiotic stress alters transcript profiles and activity of glutathione S-transferase, glutathione peroxidase, and glutathione reductase in Euphorbia esula. Physiol. Plant. 120: 421-433.
    • (2004) Physiol. Plant. , vol.120 , pp. 421-433
    • Anderson, J.V.1    Davis, D.G.2
  • 3
    • 0027236637 scopus 로고
    • A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana; molecular cloning and functional characterization
    • Bartling, D., Radzio, R., Steiner, U. and Weiler, E.W. (1993) A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana; molecular cloning and functional characterization. Eur. J. Biochem. 216: 579-586.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 579-586
    • Bartling, D.1    Radzio, R.2    Steiner, U.3    Weiler, E.W.4
  • 4
    • 0032775547 scopus 로고    scopus 로고
    • Purification and characterization of the glutathione-S-transferases from the northern quahog Mercinaria mercinaria
    • Blanchette, B.N. and Singh, B.R. (1999) Purification and characterization of the glutathione-S-transferases from the northern quahog Mercinaria mercinaria. Marine Biotechnol. 1: 74-80.
    • (1999) Marine Biotechnol. , vol.1 , pp. 74-80
    • Blanchette, B.N.1    Singh, B.R.2
  • 5
    • 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. (1976) A rapid and sensitive method for the 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
  • 6
    • 0002915845 scopus 로고    scopus 로고
    • Responses to abiotic stresses
    • Edited by Buchanan, B., Gruissem, W. and Jones, R. American Society of Plant Physiologists, MD
    • Bray, E.A., Bailey-Serres, J. and Weretilnyk, E. (2000) Responses to abiotic stresses. In Biochemistry and Molecular Biology of Plants. Edited by Buchanan, B., Gruissem, W. and Jones, R. pp. 1158-1203. American Society of Plant Physiologists, MD.
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 1158-1203
    • Bray, E.A.1    Bailey-Serres, J.2    Weretilnyk, E.3
  • 7
    • 0030300153 scopus 로고    scopus 로고
    • 2-inducible, Arabidopsis glutathione S-transferase gene contains closely linked OBF- and OBP1-binding sites
    • 2-inducible, Arabidopsis glutathione S-transferase gene contains closely linked OBF- and OBP1-binding sites. Plant J. 10: 955-966.
    • (1996) Plant J. , vol.10 , pp. 955-966
    • Chen, W.1    Chao, G.2    Singh, K.B.3
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0024488993 scopus 로고
    • The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms
    • Clark, A.G. (1989) The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms. Comp. Biochem. Physiol. 92B: 419-446.
    • (1989) Comp. Biochem. Physiol. , vol.92 B , pp. 419-446
    • Clark, A.G.1
  • 10
    • 0033136432 scopus 로고    scopus 로고
    • A role for glutathione transferases functioning as glutathione peroxidases in resistance to multiple herbicides in black grass
    • Cummins, I., Cole, D.J. and Edwards, R. (1999) A role for glutathione transferases functioning as glutathione peroxidases in resistance to multiple herbicides in black grass. Plant J. 18: 285-292.
    • (1999) Plant J. , vol.18 , pp. 285-292
    • Cummins, I.1    Cole, D.J.2    Edwards, R.3
  • 12
    • 0036202462 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • reviews 3004.1-3004.10
    • Dixon, D.P., Lapthorn, A. and Edwards, R. (2002) Plant glutathione transferases. Genome Biol. 3: reviews 3004.1-3004.10.
    • (2002) Genome Biol. , vol.3
    • Dixon, D.P.1    Lapthorn, A.2    Edwards, R.3
  • 13
    • 0030497826 scopus 로고    scopus 로고
    • Characterization of glutathione transferase and glutathione peroxidases in pea (Pisum sativum)
    • Edwards, R. (1996) Characterization of glutathione transferase and glutathione peroxidases in pea (Pisum sativum). Physiol. Plant. 98: 594-604.
    • (1996) Physiol. Plant. , vol.98 , pp. 594-604
    • Edwards, R.1
  • 14
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione S-transferases: Enzymes with multiple functions in sickness and in health
    • Edwards, R., Dixon, D.P. and Walbot, V. (2000) Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health. Trends Plant Sci. 5: 193-198.
    • (2000) Trends Plant Sci. , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 15
    • 0029142035 scopus 로고
    • A 2, 4-D-inducible glutathione S-transferase from soybean (Glycine max). Purification, characterization and induction
    • Flury, T., Adam, D. and Kreuz, K. (1995) A 2, 4-D-inducible glutathione S-transferase from soybean (Glycine max). Purification, characterization and induction. Physiol. Plant. 94: 312-318.
    • (1995) Physiol. Plant. , vol.94 , pp. 312-318
    • Flury, T.1    Adam, D.2    Kreuz, K.3
  • 16
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts; amplification using a single gene-specific oligonucleotide primer
    • Frohman, M.A., Dush, M.K. and Martin, G. (1988) Rapid production of full-length cDNAs from rare transcripts; amplification using a single gene-specific oligonucleotide primer. Proc. Natl Acad. Sci. USA 85: 8998-9002.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.3
  • 18
    • 0031853047 scopus 로고    scopus 로고
    • A Nicotiana plumbaginifolia protein labeled with an azide cytokinin agonist is a glutathione S-transferase
    • Gonneau, J., Mornet, R. and Laloue, M. (1998) A Nicotiana plumbaginifolia protein labeled with an azide cytokinin agonist is a glutathione S-transferase. Physiol. Plant. 103: 114-124.
    • (1998) Physiol. Plant. , vol.103 , pp. 114-124
    • Gonneau, J.1    Mornet, R.2    Laloue, M.3
  • 19
    • 0032114287 scopus 로고    scopus 로고
    • Isolation and characterization of glutathione S-transferase isozymes from sorghum
    • Gronwald, J.W. and Plaisance, K.L. (1998) Isolation and characterization of glutathione S-transferase isozymes from sorghum. Plant Physiol. 117: 877-892.
    • (1998) Plant Physiol. , vol.117 , pp. 877-892
    • Gronwald, J.W.1    Plaisance, K.L.2
  • 20
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-coordinately regulated defense against oxidative stress
    • Hayes, J.D. and Mclellan, L.I. (1999) Glutathione and glutathione-dependent enzymes represent a co-coordinately regulated defense against oxidative stress. Free Radical Res. 31: 273-300.
    • (1999) Free Radical Res. , vol.31 , pp. 273-300
    • Hayes, J.D.1    Mclellan, L.I.2
  • 21
    • 0027622074 scopus 로고
    • Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays)
    • Irzyk, G.P. and Fuerst, E.P. (1993) Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays). Plant Physiol. 102: 803-310.
    • (1993) Plant Physiol. , vol.102 , pp. 803-1310
    • Irzyk, G.P.1    Fuerst, E.P.2
  • 22
    • 0028604463 scopus 로고
    • An ethylene-responsive enhancer element is involved in the senescence-related expression of the carnation glutathione-S-transferase (GST1) gene
    • Itzhaki, H., Maxson, J.M. and Woodson, W.R. (1994) An ethylene-responsive enhancer element is involved in the senescence-related expression of the carnation glutathione-S-transferase (GST1) gene. Proc. Natl Acad. Sci. USA 91: 8925-8929.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8925-8929
    • Itzhaki, H.1    Maxson, J.M.2    Woodson, W.R.3
  • 23
    • 0037736768 scopus 로고    scopus 로고
    • RNA editing in hornwort chloroplasts makes more than half the genes functional
    • Kugita, M., Yamamoto, Y., Fujikawa, T., Matsumoto, T. and Yoshinaga, K. (2003) RNA editing in hornwort chloroplasts makes more than half the genes functional. Nucleic Acids Res. 31: 2417-2423.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2417-2423
    • Kugita, M.1    Yamamoto, Y.2    Fujikawa, T.3    Matsumoto, T.4    Yoshinaga, K.5
  • 24
    • 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
  • 25
    • 0037414570 scopus 로고    scopus 로고
    • Binding and protection of porphyrins by glutathione S-transferases of Zea mays L.
    • Lederer, B. and Böger, P. (2003) Binding and protection of porphyrins by glutathione S-transferases of Zea mays L. Biochim. Biophys. Acta 1621: 226-233.
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 226-233
    • Lederer, B.1    Böger, P.2
  • 27
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • Mackinney, G. (1941) Absorption of light by chlorophyll solutions. J. Biol. Chem. 140: 315-322.
    • (1941) J. Biol. Chem. , vol.140 , pp. 315-322
    • Mackinney, G.1
  • 28
    • 0024269217 scopus 로고
    • Glutathione transferases - Structure and catalytic activity
    • Mannervik, B. and Danielson, U.H. (1988) Glutathione transferases - structure and catalytic activity. Crit. Rev. Biochem. 23: 283-337.
    • (1988) Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 29
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione S-transferases in plants
    • Marrs, K.A. (1996) The functions and regulation of glutathione S-transferases in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47: 127-158.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 30
    • 0033739043 scopus 로고    scopus 로고
    • A genomics approach to the comprehensive analysis of the glutathione S-transferase gene family in soybean and maize
    • McGonigle, B., Keeler, S.J., Lau, S-M.C., Koeppe, M.K. and O'Keefe, D.P. (2000) A genomics approach to the comprehensive analysis of the glutathione S-transferase gene family in soybean and maize. Plant Physiol. 124: 1105-1120.
    • (2000) Plant Physiol. , vol.124 , pp. 1105-1120
    • McGonigle, B.1    Keeler, S.J.2    Lau, S.-M.C.3    Koeppe, M.K.4    O'Keefe, D.P.5
  • 31
    • 0142200326 scopus 로고    scopus 로고
    • Osgstu3 and osgtu4, encoding tau class glutathione S-transferase, are heavy metal- and hypoxic stress-induced and differentially salt stress-responsive in rice roots
    • Moons, A. (2003) Osgstu3 and osgtu4, encoding tau class glutathione S-transferase, are heavy metal- and hypoxic stress-induced and differentially salt stress-responsive in rice roots. FEBS Lett. 553: 427-432.
    • (2003) FEBS Lett. , vol.553 , pp. 427-432
    • Moons, A.1
  • 32
    • 0033845760 scopus 로고    scopus 로고
    • AN9, a petunia glutathione S-transferase required for anthocyanin sequestration, is a flavonoid-binding protein
    • Mueller, L., Goodman, C.D., Silady, R.A. and Walbot, V. (2000) AN9, a petunia glutathione S-transferase required for anthocyanin sequestration, is a flavonoid-binding protein. Plant Physiol. 123: 1561-1570.
    • (2000) Plant Physiol. , vol.123 , pp. 1561-1570
    • Mueller, L.1    Goodman, C.D.2    Silady, R.A.3    Walbot, V.4
  • 33
    • 0033047177 scopus 로고    scopus 로고
    • Purification and characterization of a safener-induced glutathione S-transferase from wheat (Triticum aestivum)
    • Pascal, S. and Scalla, R. (1999) Purification and characterization of a safener-induced glutathione S-transferase from wheat (Triticum aestivum). Physiol. Plant. 106: 17-27.
    • (1999) Physiol. Plant. , vol.106 , pp. 17-27
    • Pascal, S.1    Scalla, R.2
  • 34
    • 0030901644 scopus 로고    scopus 로고
    • Natural senescence of pea leaves. An activated oxygen-mediated function for peroxisomes
    • Pastori, G.M. and del Rio, L.A. (1997) Natural senescence of pea leaves. An activated oxygen-mediated function for peroxisomes. Plant Physiol. 113: 411-418.
    • (1997) Plant Physiol. , vol.113 , pp. 411-418
    • Pastori, G.M.1    Del Rio, L.A.2
  • 35
    • 0033047445 scopus 로고    scopus 로고
    • MRP subfamily ABC transporters from plants and yeast
    • Rea, P.A. (1999) MRP subfamily ABC transporters from plants and yeast. J. Exp. Bot. 50: 895-913.
    • (1999) J. Exp. Bot. , vol.50 , pp. 895-913
    • Rea, P.A.1
  • 36
    • 0034541507 scopus 로고    scopus 로고
    • Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidases
    • Roxas, V.P., Lodhi, S.A., Garrett, D.K., Mahan, J.R. and Allen, R.D. (2000) Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidases. Plant Cell Physiol. 41: 1229-1234.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1229-1234
    • Roxas, V.P.1    Lodhi, S.A.2    Garrett, D.K.3    Mahan, J.R.4    Allen, R.D.5
  • 38
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function, and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan, D., Meade, G., Foley, V.M. and Dowd, C.A. (2001) Structure, function, and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360: 1-16.
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 39
    • 0022386759 scopus 로고
    • Different forms of human liver glutathione S-transferases arise from dimeric combinations of at least four immunologically and distinct subunits
    • Singh, S.V., Dao, D.D., Partridge, C.A., Theodore, C., Srivastava, S.K. and Awasthi, Y.C. (1985) Different forms of human liver glutathione S-transferases arise from dimeric combinations of at least four immunologically and distinct subunits. Biochem. J. 232: 781-790.
    • (1985) Biochem. J. , vol.232 , pp. 781-790
    • Singh, S.V.1    Dao, D.D.2    Partridge, C.A.3    Theodore, C.4    Srivastava, S.K.5    Awasthi, Y.C.6
  • 40
    • 0035834564 scopus 로고    scopus 로고
    • Induction of new isoforms of superoxide dismutase and catalase enzymes in the flag leaf of wheat during monocarpic senescence
    • Srivalli, B. and Khanna-Chopra, R. (2001) Induction of new isoforms of superoxide dismutase and catalase enzymes in the flag leaf of wheat during monocarpic senescence. Biochem. Biophys. Res. Commun. 288: 1037-1042.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1037-1042
    • Srivalli, B.1    Khanna-Chopra, R.2
  • 42
    • 0036499691 scopus 로고    scopus 로고
    • Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the brown plant hopper, Nilaparvata lugens
    • Vontas, J.G., Small, G.J., Nikou, D.C., Ranson, H. and Hemingway, J. (2002) Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the brown plant hopper, Nilaparvata lugens. Biochem. J. 362: 329-337.
    • (2002) Biochem. J. , vol.362 , pp. 329-337
    • Vontas, J.G.1    Small, G.J.2    Nikou, D.C.3    Ranson, H.4    Hemingway, J.5
  • 43
    • 0033231547 scopus 로고    scopus 로고
    • Characterization of cDNA expressed in the early stages of microspore embryogenesis in barley (Hordeum vulgare) L.
    • Vrinten, P.L., Nakamura, T. and Kasha, K.J. (1999) Characterization of cDNA expressed in the early stages of microspore embryogenesis in barley (Hordeum vulgare) L. Plant Mol. Biol. 41: 455-463.
    • (1999) Plant Mol. Biol. , vol.41 , pp. 455-463
    • Vrinten, P.L.1    Nakamura, T.2    Kasha, K.J.3
  • 44
    • 0035983888 scopus 로고    scopus 로고
    • Probing the diversity of the Arabidopsis glutathione S-transferase gene family
    • Wagner, U., Edwards, R., Dixon, D.P. and Mauch, F. (2002) Probing the diversity of the Arabidopsis glutathione S-transferase gene family. Plant Mol. Biol. 49: 515-532.
    • (2002) Plant Mol. Biol. , vol.49 , pp. 515-532
    • Wagner, U.1    Edwards, R.2    Dixon, D.P.3    Mauch, F.4
  • 45
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce, M.C.J. and Parker, M.W. (1994) Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205: 1-18.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.J.1    Parker, M.W.2
  • 46
    • 0034525005 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of glutathione S-transferase from oat (Avena sativa) seedlings
    • Zachariah, V.T., Walsh-Sayles, N. and Singh, B.R. (2000) Isolation, purification, and characterization of glutathione S-transferase from oat (Avena sativa) seedlings. J. Protein Chem. 19: 425-430.
    • (2000) J. Protein Chem. , vol.19 , pp. 425-430
    • Zachariah, V.T.1    Walsh-Sayles, N.2    Singh, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.