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Volumn 166, Issue 2, 2004, Pages 273-283

Genetic engineering ruminal stable high methionine protein in the foliage of alfalfa

Author keywords

Alfalfa; Co expression; Rumen bypass protein; Zeins

Indexed keywords

AMINO ACIDS; GENETIC ENGINEERING; PROTEINS; VEGETATION;

EID: 1242277758     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2003.09.014     Document Type: Article
Times cited : (24)

References (43)
  • 2
    • 0000673598 scopus 로고
    • Silage and dairy cow production. III Abomasal infusions of casein, methionine and glucose, and milk yield and compositions
    • Rogers G., Bryant A., McLeay L. Silage and dairy cow production. III Abomasal infusions of casein, methionine and glucose, and milk yield and compositions. N.Z. J. Agric. Res. 22:1979;533-541.
    • (1979) N.Z. J. Agric. Res. , vol.22 , pp. 533-541
    • Rogers, G.1    Bryant, A.2    McLeay, L.3
  • 3
    • 0019837671 scopus 로고
    • Protein metabolism in growing lambs fed on fresh rye grass (Lolium perenne) white clover (Trifolium repens) pasture ad libitium
    • Barry T.N. Protein metabolism in growing lambs fed on fresh rye grass (Lolium perenne) white clover (Trifolium repens) pasture ad libitium. Br. J. Nutr. 46:1981;521-532.
    • (1981) Br. J. Nutr. , vol.46 , pp. 521-532
    • Barry, T.N.1
  • 4
    • 84970588394 scopus 로고
    • Effects of abomasal supplements of methionine on wool growth of grazing sheep
    • Pickering F.S., Reis P.J. Effects of abomasal supplements of methionine on wool growth of grazing sheep. Aust. J. Exp. Agric. 33:1993;7-12.
    • (1993) Aust. J. Exp. Agric. , vol.33 , pp. 7-12
    • Pickering, F.S.1    Reis, P.J.2
  • 6
    • 0009742247 scopus 로고
    • Selection and characterization of methionine-resistant alfalfa (M. sativa L.) cell lines
    • Reish B., Duke S.H., Bingham E.T. Selection and characterization of methionine-resistant alfalfa (M. sativa L.) cell lines. Theor. Appl. Genet. 59:1981;89-94.
    • (1981) Theor. Appl. Genet. , vol.59 , pp. 89-94
    • Reish, B.1    Duke, S.H.2    Bingham, E.T.3
  • 7
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed and degraded in the seeds of transgenic plants
    • Hoffman L.M., Donaldson D.D., Herman E.M. A modified storage protein is synthesized, processed and degraded in the seeds of transgenic plants. Plant Mol. Biol. 11:1988;717-729.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 717-729
    • Hoffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 10
  • 11
    • 0030844328 scopus 로고    scopus 로고
    • Enhanced methionine levels and increased nutritive value of seeds of transgenic lupins (Lupinus angustifolius L.) expressing a sunflower seed albumin gene
    • Molvig L., Tabe L.M., Eggum B.O., Moore A.E., Craig S., Spencer D., Higgins T.J.V. Enhanced methionine levels and increased nutritive value of seeds of transgenic lupins (Lupinus angustifolius L.) expressing a sunflower seed albumin gene. Proc. Natl. Acad. Sci. 94:1997;8393-8398.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 8393-8398
    • Molvig, L.1    Tabe, L.M.2    Eggum, B.O.3    Moore, A.E.4    Craig, S.5    Spencer, D.6    Higgins, T.J.V.7
  • 12
    • 0028123615 scopus 로고
    • A chimeric gene encoding the methionine-rich 2S albumin of the Brazil nut (Bertholletia excelsa H.B.K.) is stably expressed and inherited in transgenic grain legumes
    • Saalbach I., Pickardt T., Machemehl F., Saalbach G., Schieder O., Muntz K. A chimeric gene encoding the methionine-rich 2S albumin of the Brazil nut (Bertholletia excelsa H.B.K.) is stably expressed and inherited in transgenic grain legumes. Mol. Gen. Genet. 242:1994;226-236.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 226-236
    • Saalbach, I.1    Pickardt, T.2    MacHemehl, F.3    Saalbach, G.4    Schieder, O.5    Muntz, K.6
  • 14
    • 0030138048 scopus 로고    scopus 로고
    • Accumulation of a sulphur-rich seed albumin from sunflower in the leaves of transgenic subterraneum clover (Trifolium subterraneum L.)
    • Khan M.R.I., Ceriotti A., Tabe L., Aryan A., McNabb W., Moore A., Craig S., Spencer D., Higgins T.J.V. Accumulation of a sulphur-rich seed albumin from sunflower in the leaves of transgenic subterraneum clover (Trifolium subterraneum L.). Transgenic Res. 5:1996;179-185.
    • (1996) Transgenic Res. , vol.5 , pp. 179-185
    • Khan, M.R.I.1    Ceriotti, A.2    Tabe, L.3    Aryan, A.4    McNabb, W.5    Moore, A.6    Craig, S.7    Spencer, D.8    Higgins, T.J.V.9
  • 16
    • 0028534836 scopus 로고
    • Expression of the pea albumin 1 gene in transgenic white clover and tobacco
    • Ealing P.M., Hancock K.R., White D.W.R. Expression of the pea albumin 1 gene in transgenic white clover and tobacco. Transgen. Res. 3:1994;344-354.
    • (1994) Transgen. Res. , vol.3 , pp. 344-354
    • Ealing, P.M.1    Hancock, K.R.2    White, D.W.R.3
  • 17
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein in protein bodies of maize endosperm
    • Larkins B.A., Hurkman W.J. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 62:1978;256-263.
    • (1978) Plant Physiol. , vol.62 , pp. 256-263
    • Larkins, B.A.1    Hurkman, W.J.2
  • 19
    • 0029360630 scopus 로고
    • Determinants of the high-methionine trait in wild and exotic germplasm may have escaped selection during early cultivation of maize
    • Swarup S., Timmerman M.C., Chaudhuri S., Messing J. Determinants of the high-methionine trait in wild and exotic germplasm may have escaped selection during early cultivation of maize. Plant J. 8:1995;359-368.
    • (1995) Plant J. , vol.8 , pp. 359-368
    • Swarup, S.1    Timmerman, M.C.2    Chaudhuri, S.3    Messing, J.4
  • 20
    • 0029105386 scopus 로고
    • Accumulation of a 15-kD zein in novel protein bodies in transgenic tobacco
    • Bagga S., Adams H.P., Kemp J.D., Sengupta-Gopalan C. Accumulation of a 15-kD zein in novel protein bodies in transgenic tobacco. Plant Physiol. 107:1995;13-23.
    • (1995) Plant Physiol. , vol.107 , pp. 13-23
    • Bagga, S.1    Adams, H.P.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 21
    • 0031420939 scopus 로고    scopus 로고
    • Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein
    • Bagga S., Adams H.P., Rodriguez F.D., Kemp J.D., Sengupta-Gopalan C. Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein. Plant Cell. 9:1997;1683-1696.
    • (1997) Plant Cell , vol.9 , pp. 1683-1696
    • Bagga, S.1    Adams, H.P.2    Rodriguez, F.D.3    Kemp, J.D.4    Sengupta-Gopalan, C.5
  • 23
    • 0036803543 scopus 로고    scopus 로고
    • β-Zein protein bodies sequester and protect the 18 kDa δ-zein protein from degradation
    • Hinchliffe D.J., Kemp J.D. β-Zein protein bodies sequester and protect the 18 kDa δ-zein protein from degradation. Plant Sci. 163:2002;741-752.
    • (2002) Plant Sci. , vol.163 , pp. 741-752
    • Hinchliffe, D.J.1    Kemp, J.D.2
  • 24
    • 0031735651 scopus 로고    scopus 로고
    • Expression of a sulfur-rich maize seed srorage protein, δ-zein, in white clover (Trifolium repens) to improve forage quality
    • Sharma S.B., R Hancock K., Ealing P.M., White D.W.R. Expression of a sulfur-rich maize seed srorage protein, δ-zein, in white clover (Trifolium repens) to improve forage quality. Mol. Breed. 4:1998;435-448.
    • (1998) Mol. Breed. , vol.4 , pp. 435-448
    • Sharma, S.B.1    Hancock K, R.2    Ealing, P.M.3    White, D.W.R.4
  • 26
    • 77957060270 scopus 로고
    • Improved vectors for plant transformation: Expression cassette vector and new identifiable markers
    • Rogers S., Klee H., Horsch R., Fraley R. Improved vectors for plant transformation: expression cassette vector and new identifiable markers. Meth. Enzymol. 153:1987;253-263.
    • (1987) Meth. Enzymol. , vol.153 , pp. 253-263
    • Rogers, S.1    Klee, H.2    Horsch, R.3    Fraley, R.4
  • 27
    • 0000951724 scopus 로고
    • Production and field performance of transgenic alfalfa (Medicago Sativa L.) expressing α-amylase and manganese-dependent lignin peroxidase
    • Austin S., Bingham E.T., Mathews D.E., Shahan M.N., Will J., Burgess R.R. Production and field performance of transgenic alfalfa (Medicago Sativa L.) expressing α-amylase and manganese-dependent lignin peroxidase. Euphytica. 85:1995;381-393.
    • (1995) Euphytica , vol.85 , pp. 381-393
    • Austin, S.1    Bingham, E.T.2    Mathews, D.E.3    Shahan, M.N.4    Will, J.5    Burgess, R.R.6
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0000477510 scopus 로고
    • Diversity of abundanct mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings
    • de Vries S.C., Springer J., Wessels J.G.H. Diversity of abundanct mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings. Planta. 156:1982;129-135.
    • (1982) Planta , vol.156 , pp. 129-135
    • De Vries, S.C.1    Springer, J.2    Wessels, J.G.H.3
  • 30
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron opaque stain in electron microscopy
    • Reynolds E.S. The use of lead citrate at high pH as an electron opaque stain in electron microscopy. J. Cell Biol. 17:1963;208-212.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 32
    • 0002695212 scopus 로고    scopus 로고
    • Homology-dependent gene silencing in plants, annual review of plant physiology
    • Meyer P., Saedler H. Homology-dependent gene silencing in plants, annual review of plant physiology. Plant Mol. Biol. 47:1996;23-48.
    • (1996) Plant Mol. Biol. , vol.47 , pp. 23-48
    • Meyer, P.1    Saedler, H.2
  • 33
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin L.A. The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J. 11:1997;1151-1165.
    • (1997) Plant J. , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 34
    • 0032866269 scopus 로고    scopus 로고
    • Expression of bacterial cellulase genes in transgenic alfalfa ( Medicago sativa L.), potato ( Solanum tuberosum L.) and tobacco (Nicotiana tabacum L.)
    • Ziegelhoffer T., Will G., Austin-Phillips S. Expression of bacterial cellulase genes in transgenic alfalfa ( Medicago sativa L.), potato ( Solanum tuberosum L.) and tobacco (Nicotiana tabacum L.). Mol. Breed. 5:1999;309-318.
    • (1999) Mol. Breed , vol.5 , pp. 309-318
    • Ziegelhoffer, T.1    Will, G.2    Austin-Phillips, S.3
  • 35
    • 0036185318 scopus 로고    scopus 로고
    • Zein accumulation in forage species (Lotus corniculatus and Medicago sativa) and co-expression of the γ-zein: KDEL and β-zein: KDEL polypeptides in tobacco leaf
    • Bellucci M., Alpini A., Arcioni S. Zein accumulation in forage species (Lotus corniculatus and Medicago sativa) and co-expression of the γ-zein: KDEL and β-zein: KDEL polypeptides in tobacco leaf. Plant Cell Reprod. 20:2002;848-856.
    • (2002) Plant Cell Reprod. , vol.20 , pp. 848-856
    • Bellucci, M.1    Alpini, A.2    Arcioni, S.3
  • 36
    • 0024040378 scopus 로고
    • The digestion of perennial ryegrass (Lolium perenne cv, Melle) and white clover (Trifolium repens cv Blanca) by grazing cattle
    • Ulyatt M.J., Thomson D.J., Beever D.E., Evans R.T., Haines M.J. The digestion of perennial ryegrass (Lolium perenne cv, Melle) and white clover (Trifolium repens cv Blanca) by grazing cattle. Br. J. Nutr. 60:1988;137-149.
    • (1988) Br. J. Nutr. , vol.60 , pp. 137-149
    • Ulyatt, M.J.1    Thomson, D.J.2    Beever, D.E.3    Evans, R.T.4    Haines, M.J.5
  • 37
    • 0026931215 scopus 로고
    • Manipulation of amino acid supply to the growing ruminant
    • Merchen N.R., Trigemeyer E.C. Manipulation of amino acid supply to the growing ruminant. J. Anim. Sci. 70:1992;3238-3247.
    • (1992) J. Anim. Sci. , vol.70 , pp. 3238-3247
    • Merchen, N.R.1    Trigemeyer, E.C.2
  • 38
    • 0002410969 scopus 로고
    • Amino acid nutrition of dairy cows: Productive effects and animal requirements
    • G. PC, C. DJA (Ed.)
    • H. Rulquin, R. Verite, Amino acid nutrition of dairy cows: productive effects and animal requirements, in: G. PC, C. DJA (Ed.), Recent Advances in Animal Nutrition, 1993, pp. 57-77.
    • (1993) Recent Advances in Animal Nutrition , pp. 57-77
    • Rulquin, H.1    Verite, R.2
  • 39
    • 0023697287 scopus 로고
    • Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis
    • Spencer D., Higgins T.J.V., Freer M., Dove H., Coombe J.B. Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis. Br. J. Nutr. 60:1988;241-247.
    • (1988) Br. J. Nutr. , vol.60 , pp. 241-247
    • Spencer, D.1    Higgins, T.J.V.2    Freer, M.3    Dove, H.4    Coombe, J.B.5
  • 40
    • 0028083048 scopus 로고
    • In vitro rates of rumen proteolysis of ribulose-1,5-bisphosphate (Rubisco) from lucerne leaves, and of ovalbumin, vicilin and sunflower albumin 2S storage proteins
    • McNabb W.C., Spencer D., Higgins T.J., Barry T.N. In vitro rates of rumen proteolysis of ribulose-1,5-bisphosphate (Rubisco) from lucerne leaves, and of ovalbumin, vicilin and sunflower albumin 2S storage proteins. J. Sci. Food Agric. 64:1994;53-61.
    • (1994) J. Sci. Food Agric. , vol.64 , pp. 53-61
    • McNabb, W.C.1    Spencer, D.2    Higgins, T.J.3    Barry, T.N.4
  • 41
    • 0027137332 scopus 로고
    • Genetic engineering of grain and pasture legumes for improved nutritive value
    • Tabe L.M., Higgins C.M., McNabb W.C., Higgins T.J.V. Genetic engineering of grain and pasture legumes for improved nutritive value. Genetica. 90:1993;181-200.
    • (1993) Genetica , vol.90 , pp. 181-200
    • Tabe, L.M.1    Higgins, C.M.2    McNabb, W.C.3    Higgins, T.J.V.4
  • 42
    • 0028558460 scopus 로고
    • Identification of sulphur-rich proteins which resist rumen degradation and are hydrolysed rapidly by intestinal proteases
    • Hancock K.R., Ealing P.M., White D.R.W. Identification of sulphur-rich proteins which resist rumen degradation and are hydrolysed rapidly by intestinal proteases. Br. J. Nutr. 72:1994;855-863.
    • (1994) Br. J. Nutr. , vol.72 , pp. 855-863
    • Hancock, K.R.1    Ealing, P.M.2    White, D.R.W.3
  • 43
    • 0033791052 scopus 로고    scopus 로고
    • Accumulation of maize δ-zein and β-zein: KDEL to high levels in tobacco leaves and differential increase of BiP synthesis in transformants
    • Bellucci M., Alpini A., Paolocci F., Cong L., Arcioni S. Accumulation of maize δ-zein and β-zein: KDEL to high levels in tobacco leaves and differential increase of BiP synthesis in transformants. Theor. Appl. Genet. 101:2000;796-804.
    • (2000) Theor. Appl. Genet. , vol.101 , pp. 796-804
    • Bellucci, M.1    Alpini, A.2    Paolocci, F.3    Cong, L.4    Arcioni, S.5


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