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Volumn 45, Issue 7, 2004, Pages 864-871

The accumulation of α-zein in transgenic tobacco endosperm is stabilized by co-expression of β-zein

Author keywords

Endosperm; Maize; Protein body; Tobacco; Transgenic; Zein

Indexed keywords

ISOPROTEIN; ZEIN;

EID: 4344706600     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/pch104     Document Type: Article
Times cited : (19)

References (29)
  • 3
    • 0029105386 scopus 로고
    • Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco
    • Bagga, S., Adams, H., Kemp, J.D. and Sengupta-Gopalan, C. (1995) Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco. Plant Physiol. 107: 13-23.
    • (1995) Plant Physiol. , vol.107 , pp. 13-23
    • Bagga, S.1    Adams, H.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 4
    • 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. and Sengupta-Gopalan, C. (1997) 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: 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
  • 5
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R.S., Vitanen, P.V. and Vierling, E. (1996) Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32: 191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Vitanen, P.V.2    Vierling, E.3
  • 6
    • 0029196554 scopus 로고
    • A new methionine-rich seed storage protein from maize
    • Chui, C.F. and Falco, S.C. (1995) A new methionine-rich seed storage protein from maize. Plant Physiol. 107: 291.
    • (1995) Plant Physiol. , vol.107 , pp. 291
    • Chui, C.F.1    Falco, S.C.2
  • 8
    • 0030339563 scopus 로고    scopus 로고
    • The maize γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies in transgenic tobacco endosperm
    • Coleman, C.E., Herman, E.M., Takasaki, K. and Larkins, B.A. (1996) The maize γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies in transgenic tobacco endosperm. Plant Cell 8: 2335-2345.
    • (1996) Plant Cell , vol.8 , pp. 2335-2345
    • Coleman, C.E.1    Herman, E.M.2    Takasaki, K.3    Larkins, B.A.4
  • 9
    • 0000375871 scopus 로고    scopus 로고
    • The prolamins of maize
    • Edited by Shewry, P.R. and Casey, R. Kluwer Academic Publishers, Dordrecht
    • Coleman, C.E. and Larkins, B.A. (1998) The prolamins of maize. In Seed Proteins. Edited by Shewry, P.R. and Casey, R. pp. 109-139. Kluwer Academic Publishers, Dordrecht.
    • (1998) Seed Proteins , pp. 109-139
    • Coleman, C.E.1    Larkins, B.A.2
  • 10
    • 0000587863 scopus 로고
    • Proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.)
    • Esen, A. (1987) Proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.) J. Cereal Sci. 5: 117-128.
    • (1987) J. Cereal Sci. , vol.5 , pp. 117-128
    • Esen, A.1
  • 11
    • 0000111353 scopus 로고
    • Immunocytochemical localization of δ-zein in protein bodies of maize endosperm cells
    • Esen, A. and Stetler, D.A. (1992) Immunocytochemical localization of δ-zein in protein bodies of maize endosperm cells. Amer. J. Bot. 79: 243-248.
    • (1992) Amer. J. Bot. , vol.79 , pp. 243-248
    • Esen, A.1    Stetler, D.A.2
  • 12
    • 0027507052 scopus 로고
    • Studies of the zein-like alpha-prolamins based on an analysis of amino acid sequences: Implications for their evolution and three-dimensional structure
    • Garratt, R., Oliva, G., Caracelli, I., Leite, A. and Arruda, P. (1993) Studies of the zein-like alpha-prolamins based on an analysis of amino acid sequences: Implications for their evolution and three-dimensional structure. Proteins 15: 88-99.
    • (1993) Proteins , vol.15 , pp. 88-99
    • Garratt, R.1    Oliva, G.2    Caracelli, I.3    Leite, A.4    Arruda, P.5
  • 13
    • 0028248853 scopus 로고
    • Two structural domains mediate two sequential events in γ-zein targeting: Protein endoplasmic reticulum retention and protein body formation
    • Geli, M.I., Torrent M. and Ludevid, D. (1994) Two structural domains mediate two sequential events in γ-zein targeting: Protein endoplasmic reticulum retention and protein body formation. Plant Cell 6: 1911-1922.
    • (1994) Plant Cell , vol.6 , pp. 1911-1922
    • Geli, M.I.1    Torrent, M.2    Ludevid, D.3
  • 14
    • 0036803543 scopus 로고    scopus 로고
    • Zein protein bodies sequester and protect the 18-kDa β-zein protein from degradation
    • Hinchliffe, D.J. and Kemp, J.D. (2002) β-Zein protein bodies sequester and protect the 18-kDa β-zein protein from degradation. Plant Sci. 163: 741-752.
    • (2002) Plant Sci. , vol.163 , pp. 741-752
    • Hinchliffe, D.J.1    Kemp, J.D.2
  • 15
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed and degraded in transgenic plants
    • Hoffman, L.M., Donaldson, D.D. and Herman, E.M. (1988) A modified storage protein is synthesized, processed and degraded in transgenic plants. Plant Mol. Biol. 11: 17-29.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 17-29
    • Hoffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 16
    • 0036214280 scopus 로고    scopus 로고
    • Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm
    • Kim, C.S., Woo, Y.-M., Clore, A.M., Burnett, R.J., Carneiro, N.P. and Larkins, B.A. (2002) Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm. Plant Cell 14: 655-672.
    • (2002) Plant Cell , vol.14 , pp. 655-672
    • Kim, C.S.1    Woo, Y.-M.2    Clore, A.M.3    Burnett, R.J.4    Carneiro, N.P.5    Larkins, B.A.6
  • 17
    • 0024300553 scopus 로고
    • Isolation and sequence of a gene encoding a methionine-rich 10-kDa zein protein from maize
    • Kirihara, J.A., Petri, J.B. and Messing, J. (1988) Isolation and sequence of a gene encoding a methionine-rich 10-kDa zein protein from maize. Gene 71: 359-370.
    • (1988) Gene , vol.71 , pp. 359-370
    • Kirihara, J.A.1    Petri, J.B.2    Messing, J.3
  • 18
    • 0024740149 scopus 로고
    • Changes in the zein composition of protein bodies during maize endosperm development
    • Lending, C.R. and Larkins, B.A. (1989) Changes in the zein composition of protein bodies during maize endosperm development. Plant Cell 1: 1011-1023.
    • (1989) Plant Cell , vol.1 , pp. 1011-1023
    • Lending, C.R.1    Larkins, B.A.2
  • 19
    • 0002057478 scopus 로고
    • Structure of maize protein bodies and immunocytochemical localization of zeins
    • Lending, C.R., Kriz, A.L., Larkins, B.A. and Bracker, C.E. (1988) Structure of maize protein bodies and immunocytochemical localization of zeins. Protoplasma 143: 51-62.
    • (1988) Protoplasma , vol.143 , pp. 51-62
    • Lending, C.R.1    Kriz, A.L.2    Larkins, B.A.3    Bracker, C.E.4
  • 20
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • Levanony, H., Rubin, R., Altschuler, Y. and Galili, G. (1992) Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119: 1117-1128.
    • (1992) J. Cell Biol. , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 23
    • 0022423191 scopus 로고
    • Nucleic acid (cDNA) and amino acid sequences of the maize endosperm protein glutelin-2
    • Prat, S., Cortadas, J., Puigdomenech, P. and Palau, J. (1985) Nucleic acid (cDNA) and amino acid sequences of the maize endosperm protein glutelin-2. Nucleic Acids Res. 13: 1493-1504.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1493-1504
    • Prat, S.1    Cortadas, J.2    Puigdomenech, P.3    Palau, J.4
  • 24
    • 0023072257 scopus 로고
    • Multiple variability in the sequence of a family of maize endosperm proteins
    • Prat, S., Perez-Grau, L. and Puigdomenech, P. (1987) Multiple variability in the sequence of a family of maize endosperm proteins. Gene 52: 41-49.
    • (1987) Gene , vol.52 , pp. 41-49
    • Prat, S.1    Perez-Grau, L.2    Puigdomenech, P.3
  • 25
    • 0028894404 scopus 로고
    • Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole
    • Pueyo, J.J., Chrispeels, M.J. and Herman, E.M. (1995) Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta 196: 586-596.
    • (1995) Planta , vol.196 , pp. 586-596
    • Pueyo, J.J.1    Chrispeels, M.J.2    Herman, E.M.3
  • 26
    • 0026045554 scopus 로고
    • Analysis of the 5′ flanking region responsible for the endosperm-specific expression of a rice glutelin chimeric gene in transgenic tobacco
    • Takaiwa, F., Oono, K. and Kato, A. (1991) Analysis of the 5′ flanking region responsible for the endosperm-specific expression of a rice glutelin chimeric gene in transgenic tobacco. Plant Mol. Biol. 15: 49-58.
    • (1991) Plant Mol. Biol. , vol.15 , pp. 49-58
    • Takaiwa, F.1    Oono, K.2    Kato, A.3
  • 27
    • 0032725633 scopus 로고    scopus 로고
    • The endoplasmic reticulum-Gateway of the secretory pathway
    • Vitale, A. and Denecke, J. (1999) The endoplasmic reticulum-Gateway of the secretory pathway. Plant Cell 11: 615-628.
    • (1999) Plant Cell , vol.11 , pp. 615-628
    • Vitale, A.1    Denecke, J.2
  • 28
    • 11944254685 scopus 로고
    • New methods for extraction and quantitation of zeins reveal a high content of γ-zein in modified opaque2 maize
    • Wallace, J.C., Lopes, M.A., Paiva, E. and Larkins, B.A. (1990) New methods for extraction and quantitation of zeins reveal a high content of γ-zein in modified opaque2 maize. Plant Physiol. 92: 191-196.
    • (1990) Plant Physiol. , vol.92 , pp. 191-196
    • Wallace, J.C.1    Lopes, M.A.2    Paiva, E.3    Larkins, B.A.4
  • 29
    • 0034764976 scopus 로고    scopus 로고
    • Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression
    • Woo, Y.-M., Hu, D.W.-N., Larkins, B.A. and Jung, R. (2001) Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression. Plant Cell 13: 2297-2317.
    • (2001) Plant Cell , vol.13 , pp. 2297-2317
    • Woo, Y.-M.1    Hu, D.W.-N.2    Larkins, B.A.3    Jung, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.