메뉴 건너뛰기




Volumn 118, Issue 4, 2003, Pages 523-531

The expression of a germin-like protein with superoxide dismutase activity in the halophyte Atriplex lentiformis is differentially regulated by wounding and abscisic acid

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; DNA; IMMUNOLOGY; OLIGOMERS; ORGANIC ACIDS; RNA;

EID: 0041520874     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.2003.00133.x     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 0036001083 scopus 로고    scopus 로고
    • Role of superoxide dismutases (SODs) in controlling oxidative stress in plants
    • Alscher RG, Erturk N, Heath LS (2002) Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. J Exp Bot 53: 1331-1341
    • (2002) J Exp Bot , vol.53 , pp. 1331-1341
    • Alscher, R.G.1    Erturk, N.2    Heath, L.S.3
  • 3
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44: 276-287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 4
    • 0031081434 scopus 로고    scopus 로고
    • Regulated expression of a wheat germin gene in tobacco: Oxalate oxidase activity and apoplastic localization of the heterologous protein
    • Berna A, Bernier F (1997) Regulated expression of a wheat germin gene in tobacco: oxalate oxidase activity and apoplastic localization of the heterologous protein. Plant Mol Biol 33: 417-429
    • (1997) Plant Mol Biol , vol.33 , pp. 417-429
    • Berna, A.1    Bernier, F.2
  • 6
    • 0034913101 scopus 로고    scopus 로고
    • Germins and germin-like proteins: Plant do-all proteins. But what do they do exactly?
    • Bernier F, Berna A (2001) Germins and germin-like proteins: plant do-all proteins. But what do they do exactly? Plant Physiol Biochem 39: 545-554
    • (2001) Plant Physiol Biochem , vol.39 , pp. 545-554
    • Bernier, F.1    Berna, A.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0026735576 scopus 로고
    • Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: A novel, rapid defense response
    • Bradley DJ, Kjellbom P, Lamb CJ (1992) Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defense response. Cell 70: 21-30
    • (1992) Cell , vol.70 , pp. 21-30
    • Bradley, D.J.1    Kjellbom, P.2    Lamb, C.J.3
  • 10
    • 0029175039 scopus 로고
    • Purification and partial characterization of tomato extensin peroxidase
    • Brownleader MD, Ahmed N, Trevan M, Chaplin M, Dey PM (1995) Purification and partial characterization of tomato extensin peroxidase. Plant Physiol 109: 1115-1123
    • (1995) Plant Physiol , vol.109 , pp. 1115-1123
    • Brownleader, M.D.1    Ahmed, N.2    Trevan, M.3    Chaplin, M.4    Dey, P.M.5
  • 11
    • 0034711245 scopus 로고    scopus 로고
    • Tobacco nectarin I: Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues
    • Carter C, Thornburg RW (2000) Tobacco nectarin I: purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues. J Biol Chem 275: 36726-36733
    • (2000) J Biol Chem , vol.275 , pp. 36726-36733
    • Carter, C.1    Thornburg, R.W.2
  • 12
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S, Puryear J, Cairney J (1993) A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol Rep 11: 113-116
    • (1993) Plant Mol Biol Rep , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 13
    • 0000830127 scopus 로고    scopus 로고
    • Control of lignin biosynthesis
    • Jain SM, Minocha SC (eds), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Christensen JH, Baucher M, O'Connell A, van Montagu M, Boerjan W (2000) Control of lignin biosynthesis. In: Jain SM, Minocha SC (eds) Molecular Biology of Woody Plants, Vol. 1. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 227-267
    • (2000) Molecular Biology of Woody Plants , vol.1 , pp. 227-267
    • Christensen, J.H.1    Baucher, M.2    O'Connell, A.3    Van Montagu, M.4    Boerjan, W.5
  • 15
    • 0029073123 scopus 로고
    • Jasmonic acid distribution and action in plants: Regulation during development and response to biotic and abiotic stress
    • Creelman RA, Mullet JE (1995) Jasmonic acid distribution and action in plants: regulation during development and response to biotic and abiotic stress. Proc Natl Acad Sci USA 92: 4114-4119
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4114-4119
    • Creelman, R.A.1    Mullet, J.E.2
  • 17
    • 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 (1986) 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) Plant Physiol , vol.81 , pp. 487-492
    • Espelie, K.E.1    Franceschi, V.R.2    Kolattukudy, P.E.3
  • 18
    • 0014276538 scopus 로고
    • Nutrient requirements of suspension cultures of soybean root cells
    • Gamborg OL, Miller RA, Ojima K (1968) Nutrient requirements of suspension cultures of soybean root cells. Exp Cell Res 50: 151-158
    • (1968) Exp Cell Res , vol.50 , pp. 151-158
    • Gamborg, O.L.1    Miller, R.A.2    Ojima, K.3
  • 19
    • 0025494298 scopus 로고
    • mRNAs newly synthesized by tobacco mesophyll protoplasts are wound-inducible
    • Grosset J, Marty I, Chartier Y, Meyer Y (1990) mRNAs newly synthesized by tobacco mesophyll protoplasts are wound-inducible. Plant Mol Biol 15: 485-496
    • (1990) Plant Mol Biol , vol.15 , pp. 485-496
    • Grosset, J.1    Marty, I.2    Chartier, Y.3    Meyer, Y.4
  • 20
    • 0021668860 scopus 로고
    • Signal resistance of a soluble protein to enzymic proteolysis. An unorthodox approach to the isolation and purification of germin, a rare growth-related protein
    • Grzelczak ZF, Lane BG (1984) Signal resistance of a soluble protein to enzymic proteolysis. An unorthodox approach to the isolation and purification of germin, a rare growth-related protein. Can J Biochem Cell Biol 62: 1351-1353
    • (1984) Can J Biochem Cell Biol , vol.62 , pp. 1351-1353
    • Grzelczak, Z.F.1    Lane, B.G.2
  • 21
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B, Gutteridge JMC (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219: 1-14
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 22
    • 0000539026 scopus 로고    scopus 로고
    • Abscisic acid - A hormonal long-distance stress signal in plants under drought and salt stress
    • Pessarakli M (ed). Marcel Dekker, New York, NY
    • Hartung W, Peuke AD, Davies W (1999) Abscisic acid - a hormonal long-distance stress signal in plants under drought and salt stress. In: Pessarakli M (ed) Handbook of Plant and Crop Stress. Marcel Dekker, New York, NY, pp 731-747
    • (1999) Handbook of Plant and Crop Stress , pp. 731-747
    • Hartung, W.1    Peuke, A.D.2    Davies, W.3
  • 25
    • 0035193692 scopus 로고    scopus 로고
    • Rapid deposition of extensin during the elicitation of grapevine callus cultures is specifically catalyzed by a 40-kilodalton peroxidase
    • Jackson PAP, Galinha CIR, Pereira CS, Fortunato A, Soares NC, Amâncio SBQ, Ricardo CPP (2001) Rapid deposition of extensin during the elicitation of grapevine callus cultures is specifically catalyzed by a 40-kilodalton peroxidase. Plant Physiol 127: 1065-1076
    • (2001) Plant Physiol , vol.127 , pp. 1065-1076
    • Jackson, P.A.P.1    Galinha, C.I.R.2    Pereira, C.S.3    Fortunato, A.4    Soares, N.C.5    Amâncio, S.B.Q.6    Ricardo, C.P.P.7
  • 27
    • 0034863923 scopus 로고    scopus 로고
    • A novel superoxide dismutase with a high isoelectric point in higher plants. Expression, regulation, and protein localization
    • Karpinska B, Karlsson M, Schinkel H, Streller S, Süss K-H, Melzer M, Wingsle G (2001) A novel superoxide dismutase with a high isoelectric point in higher plants. Expression, regulation, and protein localization. Plant Physiol 126: 1668-1677
    • (2001) Plant Physiol , vol.126 , pp. 1668-1677
    • Karpinska, B.1    Karlsson, M.2    Schinkel, H.3    Streller, S.4    Süss, K.-H.5    Melzer, M.6    Wingsle, G.7
  • 28
    • 0021846481 scopus 로고
    • Analysis of N-linked oligosaccharide chains of glycoproteins on nitrocellulose sheets using lectin-peroxidase reagents
    • Kijimoto-Ochiai S, Katagiri YU, Ochiai H (1985) Analysis of N-linked oligosaccharide chains of glycoproteins on nitrocellulose sheets using lectin-peroxidase reagents. Anal Biochem 147: 222-229
    • (1985) Anal Biochem , vol.147 , pp. 222-229
    • Kijimoto-Ochiai, S.1    Katagiri, Y.U.2    Ochiai, H.3
  • 29
    • 0001026326 scopus 로고
    • Biopolyester membranes of plants: Cutin and suberin
    • Kolattukudy PE (1980) Biopolyester membranes of plants: cutin and suberin. Science 208: 990-1000
    • (1980) Science , vol.208 , pp. 990-1000
    • Kolattukudy, P.E.1
  • 30
    • 11544297023 scopus 로고
    • Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase
    • Lagrimini LM (1991) Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase. Plant Physiol 96: 577-583
    • (1991) Plant Physiol , vol.96 , pp. 577-583
    • Lagrimini, L.M.1
  • 31
    • 0000435925 scopus 로고
    • Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection
    • Lagrimini LM, Rothstein S (1987) Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection. Plant Physiol 84: 438-442
    • (1987) Plant Physiol , vol.84 , pp. 438-442
    • Lagrimini, L.M.1    Rothstein, S.2
  • 32
    • 0027161641 scopus 로고
    • Germin, a protein marker of early plant development, is an oxalate oxidase
    • Lane BG, Dunwell JM, Ray JA, Schmitt MR, Cuming AC (1993) Germin, a protein marker of early plant development, is an oxalate oxidase. J Biol Chem 268: 12239-12242
    • (1993) J Biol Chem , vol.268 , pp. 12239-12242
    • Lane, B.G.1    Dunwell, J.M.2    Ray, J.A.3    Schmitt, M.R.4    Cuming, A.C.5
  • 33
    • 0037204996 scopus 로고    scopus 로고
    • The jasmonate pathway
    • Liechti R, Farmer EE (2002) The jasmonate pathway. Science 296: 1649-1650
    • (2002) Science , vol.296 , pp. 1649-1650
    • Liechti, R.1    Farmer, E.E.2
  • 34
    • 0000318696 scopus 로고
    • Nucleotide sequence of a root-specific transcript encoding a germin-like protein from the halophyte Mesembryanthemum crystallinum
    • Michalowski CB, Bohnert HJ (1992) Nucleotide sequence of a root-specific transcript encoding a germin-like protein from the halophyte Mesembryanthemum crystallinum. Plant Physiol 100: 537-538
    • (1992) Plant Physiol , vol.100 , pp. 537-538
    • Michalowski, C.B.1    Bohnert, H.J.2
  • 35
    • 0031412446 scopus 로고    scopus 로고
    • Antagonistic effects of abscisic acid and jasmonates on salt stress-inducible transcripts in rice roots
    • Moons A, Prinsen E, Bauw G, Van Montagu M (1997) Antagonistic effects of abscisic acid and jasmonates on salt stress-inducible transcripts in rice roots. Plant Cell 9: 2243-2259
    • (1997) Plant Cell , vol.9 , pp. 2243-2259
    • Moons, A.1    Prinsen, E.2    Bauw, G.3    Van Montagu, M.4
  • 36
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15: 473-497
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 37
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PG, Goodman HM, O'Farrell PH (1977) High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12: 1133-1141
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.G.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 38
    • 0029830579 scopus 로고    scopus 로고
    • Intra- and extra-cellular localization of 'cytosolic' CuZn-superoxide desmutase in spinach leaf and hypocotyl
    • Ogawa K, Kanematsu S, Asada K (1996) Intra- and extra-cellular localization of 'cytosolic' CuZn-superoxide desmutase in spinach leaf and hypocotyl. Plant Cell Physiol 37: 790-799
    • (1996) Plant Cell Physiol , vol.37 , pp. 790-799
    • Ogawa, K.1    Kanematsu, S.2    Asada, K.3
  • 39
    • 0036006038 scopus 로고    scopus 로고
    • Copper amine oxidase expression in defense responses to wounding and Ascochyta rabiei invasion
    • Rea G, Metoui O, Infantino A, Federico R, Angelini R (2002) Copper amine oxidase expression in defense responses to wounding and Ascochyta rabiei invasion. Plant Physiol 128: 865-875
    • (2002) Plant Physiol , vol.128 , pp. 865-875
    • Rea, G.1    Metoui, O.2    Infantino, A.3    Federico, R.4    Angelini, R.5
  • 40
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld RA, Lewis VJ, Williams DE (1962) Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195: 281-283
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, V.J.2    Williams, D.E.3
  • 42
    • 0035830739 scopus 로고    scopus 로고
    • Two isoforms of a nucleotide-sugar pyrophosphatase/phosphodiesterase from barley leaves (Hordeum vulgare L.) are distinct oligomers of HvGLP1, a germin-like protein
    • Rodríguez-López M, Baroja-Fernández E, Zandueta-Criado A, Moreno-Bruna B, Muñoz FJ, Akazawa T, Pozueta-Romero J (2001) Two isoforms of a nucleotide-sugar pyrophosphatase/phosphodiesterase from barley leaves (Hordeum vulgare L.) are distinct oligomers of HvGLP1, a germin-like protein. FEBS Lett 490: 44-48
    • (2001) FEBS Lett , vol.490 , pp. 44-48
    • Rodríguez-López, M.1    Baroja-Fernández, E.2    Zandueta-Criado, A.3    Moreno-Bruna, B.4    Muñoz, F.J.5    Akazawa, T.6    Pozueta-Romero, J.7
  • 43
    • 0033389307 scopus 로고    scopus 로고
    • Transient expression of members of the germin-like gene family in epidermal cells of wheat confers disease resistance
    • Schweizer P, Christoffel A, Dudler R (1999) Transient expression of members of the germin-like gene family in epidermal cells of wheat confers disease resistance. Plant J 20: 541-552
    • (1999) Plant J , vol.20 , pp. 541-552
    • Schweizer, P.1    Christoffel, A.2    Dudler, R.3
  • 44
    • 0026146627 scopus 로고
    • Tomato extensin and extensin-like cDNAs: Structure and experession in response to wounding
    • Showalter A, Zhou J, Rumeau D, Worst S, Varner J (1991) Tomato extensin and extensin-like cDNAs: structure and experession in response to wounding. Plant Mol Biol 16: 547-565
    • (1991) Plant Mol Biol , vol.16 , pp. 547-565
    • Showalter, A.1    Zhou, J.2    Rumeau, D.3    Worst, S.4    Varner, J.5
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22: 4673-4680
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0019332677 scopus 로고
    • Relation of protein synthesis in imbibing wheat embryos to the cell-free translational capacities of bulk mRNA from dry and imbibing embryos
    • Thompson EW, Lane BG (1980) Relation of protein synthesis in imbibing wheat embryos to the cell-free translational capacities of bulk mRNA from dry and imbibing embryos. J Biol Chem 255: 5965-5970
    • (1980) J Biol Chem , vol.255 , pp. 5965-5970
    • Thompson, E.W.1    Lane, B.G.2
  • 48
    • 0030748530 scopus 로고    scopus 로고
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction. Plant J 11: 1187-1194
    • (1997) Plant J , vol.11 , pp. 1187-1194
    • Thordal-Christensen, H.1    Zhang, Z.2    Wei, Y.3    Collinge, D.B.4
  • 50
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: An early plant response to pathogen infection
    • Wojtaszek P (1997) Oxidative burst: an early plant response to pathogen infection. Biochem J 322: 681-692
    • (1997) Biochem J , vol.322 , pp. 681-692
    • Wojtaszek, P.1
  • 51
    • 0033766314 scopus 로고    scopus 로고
    • Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities
    • Woo E-J, Dunwell JM, Goodenough PW, Marvier AC, Pickersgill RW (2000) Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat Struct Biol 7: 1036-1040
    • (2000) Nat Struct Biol , vol.7 , pp. 1036-1040
    • Woo, E.-J.1    Dunwell, J.M.2    Goodenough, P.W.3    Marvier, A.C.4    Pickersgill, R.W.5
  • 52
    • 0033584947 scopus 로고    scopus 로고
    • Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata
    • Yamahara T, Shiono T, Suzuki T, Tanaka K, Takio S, Sato K, Yamazaki S, Satoh T (1999) Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata. J Biol Chem 274: 33274-33278
    • (1999) J Biol Chem , vol.274 , pp. 33274-33278
    • Yamahara, T.1    Shiono, T.2    Suzuki, T.3    Tanaka, K.4    Takio, S.5    Sato, K.6    Yamazaki, S.7    Satoh, T.8
  • 53
    • 0041681807 scopus 로고
    • Analogues of phenoxyacetic acid and the generation of calluses from seeds of indica rice
    • Yasuda T, Miyano S, Yamamoto Y, Uchida N, Yamaguchi T (1990) Analogues of phenoxyacetic acid and the generation of calluses from seeds of indica rice. Plant Cell Physiol 31: 763-766
    • (1990) Plant Cell Physiol , vol.31 , pp. 763-766
    • Yasuda, T.1    Miyano, S.2    Yamamoto, Y.3    Uchida, N.4    Yamaguchi, T.5
  • 54
    • 0003068562 scopus 로고    scopus 로고
    • Cloning of a wound-induced gene WI12 from Mesembryanthemum crystallinum (PGR 99-030)
    • Yen S-K, Chen P-C, Yen HE (1999) Cloning of a wound-induced gene WI12 from Mesembryanthemum crystallinum (PGR 99-030). Plant Physiol 119: 1147
    • (1999) Plant Physiol , vol.119 , pp. 1147
    • Yen, S.-K.1    Chen, P.-C.2    Yen, H.E.3
  • 55
    • 0034948328 scopus 로고    scopus 로고
    • Increased cysteine biosynthesis capacity of transgenic tobacco overexpressing an O-acetylserine (thiol) lyase modifies plant responses to oxidative stress
    • Youssefian S, Nakamura M, Orudgev E, Kondo N (2001) Increased cysteine biosynthesis capacity of transgenic tobacco overexpressing an O-acetylserine (thiol) lyase modifies plant responses to oxidative stress. Plant Physiol 126: 1001-1011
    • (2001) Plant Physiol , vol.126 , pp. 1001-1011
    • Youssefian, S.1    Nakamura, M.2    Orudgev, E.3    Kondo, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.