메뉴 건너뛰기




Volumn 165, Issue 6, 2003, Pages 1363-1367

Effect of iron on the expression of ascorbate peroxidase in Euglena gracilis White star

Author keywords

Ascorbate peroxidase; Euglena; Heme synthesis; Iron deficiency; Post transcriptional regulation

Indexed keywords

ANTIBODIES; CELLS; IRON;

EID: 0344496787     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2003.07.001     Document Type: Article
Times cited : (16)

References (23)
  • 1
    • 0035201585 scopus 로고    scopus 로고
    • Response of Arabidopsis to iron deficiency stress as revealed by microarray analysis
    • O. Thimm, B. Essigmann, S. Kloska, T. Altmann, T.J. Buckhout, Response of Arabidopsis to iron deficiency stress as revealed by microarray analysis, Plant Physiol. 127 (2001) 1030-1043.
    • (2001) Plant Physiol , vol.127 , pp. 1030-1043
    • Thimm, O.1    Essigmann, B.2    Kloska, S.3    Altmann, T.4    Buckhout, T.J.5
  • 2
    • 0030162524 scopus 로고    scopus 로고
    • Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant chloronerva
    • A. Herbik, A. Giritch, C. Horstmann, R. Becker, H.J. Balzer, H. Baumlein, U.W. Stephan, Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant chloronerva, Plant Physiol. 111 (1996) 533-540.
    • (1996) Plant Physiol. , vol.111 , pp. 533-540
    • Herbik, A.1    Giritch, A.2    Horstmann, C.3    Becker, R.4    Balzer, H.J.5    Baumlein, H.6    Stephan, U.W.7
  • 3
    • 0001457444 scopus 로고
    • Marked increase in ascorbate oxidase protein in pumpkin callus by adding copper
    • M. Esaka, M. Uchida, H. Fukui, K. Kubota, K. Suzuki, Marked increase in ascorbate oxidase protein in pumpkin callus by adding copper, Plant Physiol. 88 (1988) 656-660.
    • (1988) Plant Physiol. , vol.88 , pp. 656-660
    • Esaka, M.1    Uchida, M.2    Fukui, H.3    Kubota, K.4    Suzuki, K.5
  • 5
    • 0035096756 scopus 로고    scopus 로고
    • Iron deficiency differently affects peroxidase isoforms in sunflower
    • A. Ranieri, A. Castagna, B. Baldan, G.P. Soldatini, Iron deficiency differently affects peroxidase isoforms in sunflower, J. Exp. Bot. 52 (2001) 25-35.
    • (2001) J. Exp. Bot. , vol.52 , pp. 25-35
    • Ranieri, A.1    Castagna, A.2    Baldan, B.3    Soldatini, G.P.4
  • 6
    • 0030790519 scopus 로고    scopus 로고
    • Iron triggers a rapid induction of ascorbate peroxidase gene expression in Brassica napus
    • G. Vansuyt, F. Lopez, D. Inze, J.F. Briat, P Fourcroy, Iron triggers a rapid induction of ascorbate peroxidase gene expression in Brassica napus. FEBS Lett. 410 (1997) 195-200.
    • (1997) FEBS Lett. , vol.410 , pp. 195-200
    • Vansuyt, G.1    Lopez, F.2    Inze, D.3    Briat, J.F.4    Fourcroy, P.5
  • 7
    • 0035983882 scopus 로고    scopus 로고
    • Reactive oxygen intermediates and glutathione regulate the expression of cytosolic ascorbate peroxidase during iron-mediated oxidative stress in bean
    • I. Pekker, E. Tel-Or, R. Mittler. Reactive oxygen intermediates and glutathione regulate the expression of cytosolic ascorbate peroxidase during iron-mediated oxidative stress in bean, Plant Mol. Biol. 49 (2002) 429-438.
    • (2002) Plant Mol. Biol. , vol.49 , pp. 429-438
    • Pekker, I.1    Tel-Or, E.2    Mittler, R.3
  • 8
    • 0027132150 scopus 로고
    • Requirement for iron and its effect on ascorbate peroxidase in Euglena gracilis
    • T. Ishikawa, T. Takeda, S. Shigeoka, O. Hirayama, T. Mitsunaga, Requirement for iron and its effect on ascorbate peroxidase in Euglena gracilis, Plant Sci. 93 (1993) 25-29.
    • (1993) Plant Sci. , vol.93 , pp. 25-29
    • Ishikawa, T.1    Takeda, T.2    Shigeoka, S.3    Hirayama, O.4    Mitsunaga, T.5
  • 9
    • 0019324583 scopus 로고
    • Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase
    • S. Shigeoka, Y. Nakano, S. Kitaoka, Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase, Biochem. J. 186 (1980) 377-380.
    • (1980) Biochem. J. , vol.186 , pp. 377-380
    • Shigeoka, S.1    Nakano, Y.2    Kitaoka, S.3
  • 10
    • 0026591871 scopus 로고
    • Requirement for endogenous iron cytotoxicity caused by hydrogen peroxide in Euglena gracilis
    • K. Radtke, R.W. Byrnes, P. Kerrigan, W.E. Antholine, D.H. Petering, Requirement for endogenous iron cytotoxicity caused by hydrogen peroxide in Euglena gracilis, Mar. Environ. Res. 34 (1992) 339-343.
    • (1992) Mar. Environ. Res. , vol.34 , pp. 339-343
    • Radtke, K.1    Byrnes, R.W.2    Kerrigan, P.3    Antholine, W.E.4    Petering, D.H.5
  • 11
    • 0002716872 scopus 로고
    • High-yield media for photosynthesizing Euglena gracilis Z
    • L.E. Koren, S.H. Hutner, High-yield media for photosynthesizing Euglena gracilis Z, J. Protozool. 14 (1967) 17.
    • (1967) J. Protozool. , vol.14 , pp. 17
    • Koren, L.E.1    Hutner, S.H.2
  • 12
    • 0038734441 scopus 로고    scopus 로고
    • Characterization of an ascorbate peroxidase in plastids of tobacco BY-2 cells
    • R. Madhusudhan, T. Ishikawa, Y Sawa, S. Shigeoka, H. Shibata, Characterization of an ascorbate peroxidase in plastids of tobacco BY-2 cells, Physiol. Plant. 117 (2003) 550-557.
    • (2003) Physiol. Plant. , vol.117 , pp. 550-557
    • Madhusudhan, R.1    Ishikawa, T.2    Sawa, Y.3    Shigeoka, S.4    Shibata, H.5
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0029895579 scopus 로고
    • Molecular characterization of Euglena ascorbate peroxidase using monoclonal antibody
    • T. Ishikawa, T. Takeda, H. Kohno, S. Shigeoka, Molecular characterization of Euglena ascorbate peroxidase using monoclonal antibody, Biochim. Biophys. Acta. 1290 (1996) 69-75.
    • (1290) Biochim. Biophys. Acta. , vol.1996 , pp. 69-75
    • Ishikawa, T.1    Takeda, T.2    Kohno, H.3    Shigeoka, S.4
  • 15
    • 0038419969 scopus 로고    scopus 로고
    • Post-transcriptional regulation of ascorbate peroxidase during light adaptation of Euglena gracilis
    • R. Madhusudhan, T. Ishikawa, Y. Sawa, S. Shigeoka, H. Shibata, Post-transcriptional regulation of ascorbate peroxidase during light adaptation of Euglena gracilis, Plant Sci. 165 (2003) 233-238.
    • (2003) Plant Sci. , vol.165 , pp. 233-238
    • Madhusudhan, R.1    Ishikawa, T.2    Sawa, Y.3    Shigeoka, S.4    Shibata, H.5
  • 18
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • T.D. Rae, P.J. Schmidt, R.A. Pufahl, V.C. Culotta, T.V. O'Halloran, Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase, Science 284 (1999) 805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 20
    • 0035091725 scopus 로고    scopus 로고
    • Analysis of Euglena gracilis alpha-, beta-, and gamma-tubulin genes: Introns and pre-mRNA maturation
    • J. Canaday, L.H. Tessier, P. Imbault, F. Paulus, Analysis of Euglena gracilis alpha-, beta-, and gamma-tubulin genes: introns and pre-mRNA maturation, Mol. Genet. Genomics 265 (2001) 153-160.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 153-160
    • Canaday, J.1    Tessier, L.H.2    Imbault, P.3    Paulus, F.4
  • 22
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein
    • H. Beinert, M.C. Kennedy, C.D. Stout, Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein, Chem. Rev. 96 (1996) 2335-2374.
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 23
    • 0037474331 scopus 로고    scopus 로고
    • Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis elegans
    • B.L. Gourley, S.B. Parker, B.J. Jones, K.B. Zumbrennen, E.A. Leibold, Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis elegans, J. Biol. Chem. 278 (2003) 3227-3234.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3227-3234
    • Gourley, B.L.1    Parker, S.B.2    Jones, B.J.3    Zumbrennen, K.B.4    Leibold, E.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.