메뉴 건너뛰기




Volumn 55, Issue 404, 2004, Pages 1889-1901

Sulphur and nitrogen nutrition influence the response of chickpea seeds to an added, transgenic sink for organic sulphur

Author keywords

Amino acid; Metabolism; Modification; Nutritive value; Plant; Seed; Sulphur

Indexed keywords

AMINO ACIDS; COMPOSITION; NITROGEN; NUTRITION; PLANTS (BOTANY); PROTEINS; SULFUR;

EID: 4344570204     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/erh198     Document Type: Conference Paper
Times cited : (69)

References (50)
  • 1
    • 0017235549 scopus 로고
    • The trypsin and chymotrypsin inhibitors in chick peas (Cicer arietinum L). Identification of the trypsin-reactive site, partial-amino-acid sequence and further physicochemical properties of the major inhibitor
    • Belew M, Eaker D. 1976. The trypsin and chymotrypsin inhibitors in chick peas (Cicer arietinum L). Identification of the trypsin-reactive site, partial-amino-acid sequence and further physicochemical properties of the major inhibitor. European Journal of Biochemistry 62, 499-508.
    • (1976) European Journal of Biochemistry , vol.62 , pp. 499-508
    • Belew, M.1    Eaker, D.2
  • 2
    • 0016712817 scopus 로고
    • The trypsin and chymotrypsin inhibitors in chickpeas (Cicer arietinum L.). Purification and properties of the inhibitors
    • Belew M, Porath J, Sundberg L. 1975. The trypsin and chymotrypsin inhibitors in chickpeas (Cicer arietinum L.). Purification and properties of the inhibitors. European Journal of Biochemistry 60, 247-258.
    • (1975) European Journal of Biochemistry , vol.60 , pp. 247-258
    • Belew, M.1    Porath, J.2    Sundberg, L.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0000363398 scopus 로고
    • Methionine analogs inhibit production of beta -subunit of soybean 7S protein
    • Creason GL, Thompson JF, Madison JT. 1985. Methionine analogs inhibit production of beta -subunit of soybean 7S protein. Phytochemistry 24, 1147-1150.
    • (1985) Phytochemistry , vol.24 , pp. 1147-1150
    • Creason, G.L.1    Thompson, J.F.2    Madison, J.T.3
  • 8
    • 0032558460 scopus 로고    scopus 로고
    • Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine
    • Curien G, Job D, Douce R, Dumas R. 1998. Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine. Biochemistry 37, 13212-13221.
    • (1998) Biochemistry , vol.37 , pp. 13212-13221
    • Curien, G.1    Job, D.2    Douce, R.3    Dumas, R.4
  • 9
    • 0028847866 scopus 로고
    • Methionine biosynthesis in higher plants. II. Purification and characterization of cystathionine beta-lyase from spinach chloroplasts
    • Droux M, Ravanel S, Douce R. 1995. Methionine biosynthesis in higher plants. II. Purification and characterization of cystathionine beta-lyase from spinach chloroplasts. Archives of Biochemistry and Biophysics 316, 585-595.
    • (1995) Archives of Biochemistry and Biophysics , vol.316 , pp. 585-595
    • Droux, M.1    Ravanel, S.2    Douce, R.3
  • 10
    • 0000983901 scopus 로고
    • Effects of nutritional stress on the storage proteins of soybeans
    • Gayler KR, Sykes GE. 1985. Effects of nutritional stress on the storage proteins of soybeans. Plant Physiology 78, 582-585.
    • (1985) Plant Physiology , vol.78 , pp. 582-585
    • Gayler, K.R.1    Sykes, G.E.2
  • 11
    • 0038477091 scopus 로고    scopus 로고
    • The redistribution of protein sulphur in transgenic rice expressing a gene for a foreign, sulphur-rich protein
    • Hagan ND, Upadhyaya N, Tabe LM, Higgins TJ. 2003. The redistribution of protein sulphur in transgenic rice expressing a gene for a foreign, sulphur-rich protein. The Plant Journal 34, 1-11.
    • (2003) The Plant Journal , vol.34 , pp. 1-11
    • Hagan, N.D.1    Upadhyaya, N.2    Tabe, L.M.3    Higgins, T.J.4
  • 12
    • 0028500170 scopus 로고
    • The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation
    • Hajdukiewicz P, Svab Z, Maliga P. 1994. The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Molecular Biology 25, 989-994.
    • (1994) Plant Molecular Biology , vol.25 , pp. 989-994
    • Hajdukiewicz, P.1    Svab, Z.2    Maliga, P.3
  • 13
    • 0033979764 scopus 로고    scopus 로고
    • Plant responses to sulphur deficiency and the genetic manipulation of sulphate transporters to improve S-utilization efficiency
    • Hawkesford MJ. 2000. Plant responses to sulphur deficiency and the genetic manipulation of sulphate transporters to improve S-utilization efficiency. Journal of Experimental Botany 51, 131-138.
    • (2000) Journal of Experimental Botany , vol.51 , pp. 131-138
    • Hawkesford, M.J.1
  • 17
    • 0036127824 scopus 로고    scopus 로고
    • Independent roles of methionine and O-acetyl-L-serine in the regulation of the beta-subunit gene of beta-conglycinin
    • Hirai MY, Kim H, Hayashi H, Chino M, Naito S, Fujiwara T. 2002. Independent roles of methionine and O-acetyl-L-serine in the regulation of the beta-subunit gene of beta-conglycinin. Soil Science and Plant Nutrition 48, 87-94.
    • (2002) Soil Science and Plant Nutrition , vol.48 , pp. 87-94
    • Hirai, M.Y.1    Kim, H.2    Hayashi, H.3    Chino, M.4    Naito, S.5    Fujiwara, T.6
  • 18
    • 0000827216 scopus 로고
    • Studies on the mechanism of regulation of the mRNA level for a soybean storage protein subunit by exogenous L-methionine
    • Holowach LP, Madison JT, Thompson JF. 1986. Studies on the mechanism of regulation of the mRNA level for a soybean storage protein subunit by exogenous L-methionine. Plant Physiology 80, 561-567.
    • (1986) Plant Physiology , vol.80 , pp. 561-567
    • Holowach, L.P.1    Madison, J.T.2    Thompson, J.F.3
  • 19
    • 0001509655 scopus 로고
    • Effects of exogenous methionine on storage protein composition of soybean cotyledons cultured in vitro
    • Holowach LP, Thompson JF, Madison JT. 1984a. Effects of exogenous methionine on storage protein composition of soybean cotyledons cultured in vitro. Plant Physiology 74, 576-583.
    • (1984) Plant Physiology , vol.74 , pp. 576-583
    • Holowach, L.P.1    Thompson, J.F.2    Madison, J.T.3
  • 20
    • 0001591556 scopus 로고
    • Storage protein composition of soybean cotyledons grown in vitro in media of various sulfate concentrations in the presence and absence of exogenous L-methionine
    • Holowach LP, Thompson JF, Madison JT. 1984b. Storage protein composition of soybean cotyledons grown in vitro in media of various sulfate concentrations in the presence and absence of exogenous L-methionine. Plant Physiology 74, 584-589.
    • (1984) Plant Physiology , vol.74 , pp. 584-589
    • Holowach, L.P.1    Thompson, J.F.2    Madison, J.T.3
  • 21
    • 4344696121 scopus 로고    scopus 로고
    • Expression of a sulphur-rich protein in soybean seeds causes an altered seed protein composition
    • Proceedings of the 5th International Congress of Plant Molecular Biology
    • Jung R, Martino-Catt S, Townsend J, Beach L. 1997. Expression of a sulphur-rich protein in soybean seeds causes an altered seed protein composition. Proceedings of the 5th International Congress of Plant Molecular Biology. Plant Molecular Biology Reporter 15, (Supplement), 307.
    • (1997) Plant Molecular Biology Reporter , vol.15 , Issue.SUPPL. , pp. 307
    • Jung, R.1    Martino-Catt, S.2    Townsend, J.3    Beach, L.4
  • 22
    • 0033199730 scopus 로고    scopus 로고
    • Role of O-acetyl-L-serine in the co-ordinated regulation of the expression of a soybean seed storage-protein gene by sulfur and nitrogen nutrition
    • Kim H, Hirai MY, Hayashi H, Chino M, Naito S, Fujiwara T. 1999. Role of O-acetyl-L-serine in the co-ordinated regulation of the expression of a soybean seed storage-protein gene by sulfur and nitrogen nutrition. Planta 209, 282-289.
    • (1999) Planta , vol.209 , pp. 282-289
    • Kim, H.1    Hirai, M.Y.2    Hayashi, H.3    Chino, M.4    Naito, S.5    Fujiwara, T.6
  • 23
    • 85047686305 scopus 로고    scopus 로고
    • Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine
    • Kim J, Lee M, Chalam R, Martin MN, Leustek T, Boerjan W. 2002. Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine. Plant Physiology 128, 95-107.
    • (2002) Plant Physiology , vol.128 , pp. 95-107
    • Kim, J.1    Lee, M.2    Chalam, R.3    Martin, M.N.4    Leustek, T.5    Boerjan, W.6
  • 25
    • 0026029034 scopus 로고
    • Amino acid and cDNA sequences of a methionine-rich 2S protein from sunflower seed (Helianthus annuus L.)
    • Kortt A, Caldwell JB, Lilley GG, Higgins TJV. 1991. Amino acid and cDNA sequences of a methionine-rich 2S protein from sunflower seed (Helianthus annuus L.). European Journal of Biochemistry 195, 329-334.
    • (1991) European Journal of Biochemistry , vol.195 , pp. 329-334
    • Kortt, A.1    Caldwell, J.B.2    Lilley, G.G.3    Higgins, T.J.V.4
  • 26
    • 0031417273 scopus 로고    scopus 로고
    • 2- uptake, and oxidative stress response in intact canola roots
    • 2- uptake, and oxidative stress response in intact canola roots. Plant Physiology 114, 177-183.
    • (1997) Plant Physiology , vol.114 , pp. 177-183
    • Lappartient, A.G.1    Touraine, B.2
  • 27
    • 0033119341 scopus 로고    scopus 로고
    • Inter-organ signalling in plants: Regulation of ATP sulphurylase and sulphate transporter genes expression in roots mediated by phloem-translocated compound
    • Lappartient AG, Vidmar JJ, Leustek T, Glass ADM, Touraine B. 1999. Inter-organ signalling in plants: regulation of ATP sulphurylase and sulphate transporter genes expression in roots mediated by phloem-translocated compound. The Plant Journal 18, 89-95.
    • (1999) The Plant Journal , vol.18 , pp. 89-95
    • Lappartient, A.G.1    Vidmar, J.J.2    Leustek, T.3    Glass, A.D.M.4    Touraine, B.5
  • 28
    • 0032841269 scopus 로고    scopus 로고
    • Sulfate transport and assimilation in plants
    • Leustek T, Saito K. 1999. Sulfate transport and assimilation in plants. Plant Physiology 120, 637-643.
    • (1999) Plant Physiology , vol.120 , pp. 637-643
    • Leustek, T.1    Saito, K.2
  • 29
    • 4344627469 scopus 로고
    • Differential effect of sulphur deficiency on the composition of the aminoacyl-tRNA and free amino acid pools of the developing pea seed
    • Macnicol PK. 1983. Differential effect of sulphur deficiency on the composition of the aminoacyl-tRNA and free amino acid pools of the developing pea seed. FEBS Letters 156, 55-57.
    • (1983) FEBS Letters , vol.156 , pp. 55-57
    • Macnicol, P.K.1
  • 31
    • 0001171132 scopus 로고
    • Alteration to grain, flour and dough quality in three wheat types with variation in soil sulfur supply
    • Moss HJ, Randall PJ, Wrigley CW. 1983. Alteration to grain, flour and dough quality in three wheat types with variation in soil sulfur supply. Journal of Cereal Science 1, 255-264.
    • (1983) Journal of Cereal Science , vol.1 , pp. 255-264
    • Moss, H.J.1    Randall, P.J.2    Wrigley, C.W.3
  • 34
    • 0002798546 scopus 로고
    • Cotyledonary storage proteins in Pisum sativum. 4. Effects of sulphur, phosphorus, potassium and magnesium deficiencies
    • Randall PJ, Thomson JA, Schroeder HE. 1979. Cotyledonary storage proteins in Pisum sativum. 4. Effects of sulphur, phosphorus, potassium and magnesium deficiencies. Australian Journal of Plant Physiology 6, 11-24.
    • (1979) Australian Journal of Plant Physiology , vol.6 , pp. 11-24
    • Randall, P.J.1    Thomson, J.A.2    Schroeder, H.E.3
  • 35
    • 0034078554 scopus 로고    scopus 로고
    • Regulation of sulphate transport and synthesis of sulphur-containing amino acids
    • Saito K. 2000. Regulation of sulphate transport and synthesis of sulphur-containing amino acids. Current Opinions in Plant Biology 3, 188-195.
    • (2000) Current Opinions in Plant Biology , vol.3 , pp. 188-195
    • Saito, K.1
  • 37
    • 0020158221 scopus 로고
    • Quantitative studies on the cotyledonary proteins in the genus Pisum
    • Schroeder HE. 1982. Quantitative studies on the cotyledonary proteins in the genus Pisum. Journal of the Science of Food and Agriculture 33, 623-633.
    • (1982) Journal of the Science of Food and Agriculture , vol.33 , pp. 623-633
    • Schroeder, H.E.1
  • 38
    • 0031846553 scopus 로고    scopus 로고
    • Sulphur availability, cotyledon nitrogen:sulphur ratio, and relative abundance of seed storage proteins of soybean
    • Sexton PJ, Naeve SL, Paek NC, Shibles R. 1998. Sulphur availability, cotyledon nitrogen:sulphur ratio, and relative abundance of seed storage proteins of soybean. Crop Science 38, 983-986.
    • (1998) Crop Science , vol.38 , pp. 983-986
    • Sexton, P.J.1    Naeve, S.L.2    Paek, N.C.3    Shibles, R.4
  • 41
    • 0004579309 scopus 로고
    • Pulse-labeling studies on protein synthesis in developing pea seeds and evidence of a precursor form of legumin small subunit
    • Spencer D, Higgins TJV, Button SC, Davey RA. 1980. Pulse-labeling studies on protein synthesis in developing pea seeds and evidence of a precursor form of legumin small subunit. Plant Physiology 66, 510-515.
    • (1980) Plant Physiology , vol.66 , pp. 510-515
    • Spencer, D.1    Higgins, T.J.V.2    Button, S.C.3    Davey, R.A.4
  • 42
    • 0036011080 scopus 로고    scopus 로고
    • Plasticity of seed protein composition in response to nitrogen and sulphur availability
    • Tabe L, Hagan N, Higgins T. 2002. Plasticity of seed protein composition in response to nitrogen and sulphur availability. Current Opinions in Plant Biology 5, 212-217.
    • (2002) Current Opinions in Plant Biology , vol.5 , pp. 212-217
    • Tabe, L.1    Hagan, N.2    Higgins, T.3
  • 43
    • 0032127583 scopus 로고    scopus 로고
    • Engineering plant protein composition for improved nutrition
    • Tabe L, Higgins TJV. 1998. Engineering plant protein composition for improved nutrition. Trends in Plant Science 3, 282-286.
    • (1998) Trends in Plant Science , vol.3 , pp. 282-286
    • Tabe, L.1    Higgins, T.J.V.2
  • 44
    • 0036006062 scopus 로고    scopus 로고
    • Limits to sulphur accumulation in transgenic lupin seeds expressing a foreign sulphur-rich protein
    • Tabe LM, Droux M. 2002. Limits to sulphur accumulation in transgenic lupin seeds expressing a foreign sulphur-rich protein. Plant Physiology 128, 1137-1148.
    • (2002) Plant Physiology , vol.128 , pp. 1137-1148
    • Tabe, L.M.1    Droux, M.2
  • 45
    • 0034970544 scopus 로고    scopus 로고
    • Sulphur assimilation in developing lupin cotyledons could contribute significantly to the accumulation of organic sulphur reserves in the seed
    • Tabe LM, Droux M. 2001. Sulphur assimilation in developing lupin cotyledons could contribute significantly to the accumulation of organic sulphur reserves in the seed. Plant Physiology 126, 176-187.
    • (2001) Plant Physiology , vol.126 , pp. 176-187
    • Tabe, L.M.1    Droux, M.2
  • 47
    • 0033890171 scopus 로고    scopus 로고
    • The roles of three functional sulphate transporters involved in uptake and translocation of sulphate in Arabidopsis thaliana
    • Takahashi H, Watanabe-Takahashi A, Smith FW, Blake-Kalff M, Hawkesford MJ, Saito K. 2000. The roles of three functional sulphate transporters involved in uptake and translocation of sulphate in Arabidopsis thaliana. The Plant Journal 23, 171-182.
    • (2000) The Plant Journal , vol.23 , pp. 171-182
    • Takahashi, H.1    Watanabe-Takahashi, A.2    Smith, F.W.3    Blake-Kalff, M.4    Hawkesford, M.J.5    Saito, K.6
  • 49
    • 5744235228 scopus 로고
    • Trypsinogens and trypsins of various species
    • Perlmann GE, Lorand L, eds. New York: Academic Press
    • Walsh KA. 1970. Trypsinogens and trypsins of various species. In: Perlmann GE, Lorand L, eds. Proteolytic enzymes. New York: Academic Press, 41-63.
    • (1970) Proteolytic Enzymes , pp. 41-63
    • Walsh, K.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.