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Volumn 163, Issue 4, 2002, Pages 741-752

β-zein protein bodies sequester and protect the 18-kDa δ-zein protein from degradation

Author keywords

Co expression; Degradation; Prolamin; Pulse chase; Zein

Indexed keywords

AMINO ACIDS; DEGRADATION; DNA; GENES; TISSUE; TOBACCO; ZEIN;

EID: 0036803543     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(02)00177-2     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein in the protein bodies of maize endosperm
    • B.A. Larkins, W.J. Hurkman, Synthesis and deposition of zein in the 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
  • 2
    • 0024651681 scopus 로고
    • Structural elements regulating zein gene expression
    • G.A. Thompson, B.A. Larkins, Structural elements regulating zein gene expression, Bioessays 10 (1987) 108-113.
    • (1987) Bioessays , vol.10 , pp. 108-113
    • Thompson, G.A.1    Larkins, B.A.2
  • 3
    • 0023072257 scopus 로고
    • Multiple variability in the sequence of a family of maize endosperm proteins
    • S. Prat, L. Perez-Grau, P. Muidomenech, Multiple variability in the sequence of a family of maize endosperm proteins, Gene 52 (1987) 41-49.
    • (1987) Gene , vol.52 , pp. 41-49
    • Prat, S.1    Perez-Grau, L.2    Muidomenech, P.3
  • 4
    • 0024740149 scopus 로고
    • Changes in the zein composition of protein bodies during maize endosperm development
    • C.R. Lending, B.A. Larkins, Changes in the zein composition of protein bodies during maize endosperm development, Plant Cell 1 (1989) 1011-1023.
    • (1989) Plant Cell , vol.1 , pp. 1011-1023
    • Lending, C.R.1    Larkins, B.A.2
  • 5
    • 0034764976 scopus 로고    scopus 로고
    • Genornics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression
    • Y.M. Woo, D.W. Hu, B.A. Larkins, R. Jung, Genornics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression, Plant Cell 13 (2001) 2297-2317.
    • (2001) Plant Cell , vol.13 , pp. 2297-2317
    • Woo, Y.M.1    Hu, D.W.2    Larkins, B.A.3    Jung, R.4
  • 6
    • 0023968896 scopus 로고
    • Differential expression of a gene for a methionine-rich storage protein in maize
    • J.A. Kirihara, J.P. Hunsperger, W.C. Mahoney, J.W. Messing, Differential expression of a gene for a methionine-rich storage protein in maize, Mol. Gen. Genet. 211 (1988) 477-484.
    • (1988) Mol. Gen. Genet. , vol.211 , pp. 477-484
    • Kirihara, J.A.1    Hunsperger, J.P.2    Mahoney, W.C.3    Messing, J.W.4
  • 7
    • 0029360630 scopus 로고
    • Determinants of the high-methionine trait in wild and exotic germplasm may have escaped selection during early cultivation of maize
    • S. Swamp, M.C. Timmermans, S. Chaudhuri, J. Messing, 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
    • Swamp, S.1    Timmermans, M.C.2    Chaudhuri, S.3    Messing, J.4
  • 8
    • 0029196554 scopus 로고
    • A new methionine-rich seed storage protein from maize
    • C.F. Chui, S.C. Falco, A new methionine-rich seed storage protein from maize, Plant Physiol. 107 (1995) 291.
    • (1995) Plant Physiol. , vol.107 , pp. 291
    • Chui, C.F.1    Falco, S.C.2
  • 9
    • 0029328357 scopus 로고
    • Seed storage proteins, structures and biosynthesis
    • P.R. Shewry, J.A. Napier, A.S. Tatham, Seed storage proteins, structures and biosynthesis, Plant Cell. 7 (1995) 945-956.
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 10
    • 0026041879 scopus 로고
    • Maternal effect on high methionine Levels in hybrid corn
    • J.W. Messing, H. Fisher, Maternal effect on high methionine Levels in hybrid corn, J. Biotechnol. 21 (1991) 229-238.
    • (1991) J. Biotechnol. , vol.21 , pp. 229-238
    • Messing, J.W.1    Fisher, H.2
  • 11
    • 77957060270 scopus 로고
    • Improved vectors for plant transformation: Expression cassette vectors and new selectable markers
    • S.G. Rogers, H.J. Klee, R.B. Horsch, R.T. Fraley, Improved vectors for plant transformation: Expression cassette vectors and new selectable markers, Methods Enzymol. 153 (1987) 253-294.
    • (1987) Methods Enzymol. , vol.153 , pp. 253-294
    • Rogers, S.G.1    Klee, H.J.2    Horsch, R.B.3    Fraley, R.T.4
  • 13
    • 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
    • S. Bagga, H.P. Adams, F.D. Rodriguez, J.D. Kemp, C. Sengupta-Gopalan, 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
  • 15
    • 0001548504 scopus 로고
    • The localization by electron microscopy of HeLa cell surface enzymes splitting adenosine triphosphate
    • M.A. Epstein, S.J. Holt, The localization by electron microscopy of HeLa cell surface enzymes splitting adenosine triphosphate, J. Cell. Biol. 19 (1963) 325-326.
    • (1963) J. Cell. Biol. , vol.19 , pp. 325-326
    • Epstein, M.A.1    Holt, S.J.2
  • 16
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electronopaque stain in electron microscopy
    • E.S. Reynolds, The use of lead citrate at high pH as an electronopaque stain in electron microscopy, J. Cell. Biol. 17 (1963) 208-212.
    • (1963) J. Cell. Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 17
    • 0030339563 scopus 로고    scopus 로고
    • The maize γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm
    • C.E. Coleman, E.M. Herman, K. Takasaki, B.A. Larkins, The maize γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm, Plant Cell 8 (1996) 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
  • 18
    • 0034645802 scopus 로고    scopus 로고
    • A modified 10-kDa zein protein produces two morphologically distinct protein bodies in tratisgenic tobacco
    • J. Randall, S. Bagga, H. Adams, J.D. Kemp, A modified 10-kDa zein protein produces two morphologically distinct protein bodies in tratisgenic tobacco, Plant Sci. 150 (2000) 21-28.
    • (2000) Plant Sci. , vol.150 , pp. 21-28
    • Randall, J.1    Bagga, S.2    Adams, H.3    Kemp, J.D.4
  • 19
    • 0029105386 scopus 로고
    • Accumulation of 15-kDa zein in novel protein bodies in transgenic tobacco
    • S. Bagga, H. Adams, J.D. Kemp, C. Sengupta-Gopalan, Accumulation of 15-kDa 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.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 21
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • H. Levanony, R. Rubin, Y. Altschuler, G. Galili, Evidence for a novel route of wheat storage proteins to vacuoles, J. Cell. Biol. 119 (1992) 1117-1128.
    • (1992) J. Cell. Biol. , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 22
    • 0033840913 scopus 로고    scopus 로고
    • Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organdlle, precursor protease vesicles
    • M.J. Chrispeels, E.M. Herman, Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organdlle, precursor protease vesicles, Plant Physiol. 123 (2000) 1227-1234.
    • (2000) Plant Physiol. , vol.123 , pp. 1227-1234
    • Chrispeels, M.J.1    Herman, E.M.2
  • 25
    • 0027013660 scopus 로고
    • Amino acid limitation and flow to duodenum at four stages of lactation 1. Sequence of lysine and methionine limitation
    • C.G. Schwab, C.K. Bozak, N.L. Whitehouse, M.M. Mesbah, Amino acid limitation and flow to duodenum at four stages of lactation 1. Sequence of lysine and methionine limitation, J. Dairy Sci. 75 (1992) 3486-3502.
    • (1992) J. Dairy Sci. , vol.75 , pp. 3486-3502
    • Schwab, C.G.1    Bozak, C.K.2    Whitehouse, N.L.3    Mesbah, M.M.4
  • 27
    • 2142774259 scopus 로고    scopus 로고
    • A genetic engineering approach for improving protein quality of forage legumes
    • K.K. Tiwari, G.S. Singhal (Eds.), Narosa Publishers
    • S. Bagga, S.J. Temple, J.D. Kemp, C. Sengupta-Gopalan, A genetic engineering approach for improving protein quality of forage legumes, in: K.K. Tiwari, G.S. Singhal (Eds.), Plant Molecular Biology and Biotechnology, Narosa Publishers, 1997, pp. 304-318.
    • (1997) Plant Molecular Biology and Biotechnology , pp. 304-318
    • Bagga, S.1    Temple, S.J.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 28
    • 0026436250 scopus 로고
    • Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine
    • S.B. Altenbach, C.C. Kuo, L.C. Staraci, K.W. Pearson, C. Wainwright, A. Georgescu, J. Townsend, Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine, Plant Mol. Biol. 18 (1992) 235-245.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 235-245
    • Altenbach, S.B.1    Kuo, C.C.2    Staraci, L.C.3    Pearson, K.W.4    Wainwright, C.5    Georgescu, A.6    Townsend, J.7
  • 30
    • 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
    • L. Molvig, L.M. Tabe, B.O. Eggum, A.E. Moore, S. Craig, D. Spencer, T.J. Higgins, 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. USA 94 (1997) 3393-8398.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3393-8398
    • Molvig, L.1    Tabe, L.M.2    Eggum, B.O.3    Moore, A.E.4    Craig, S.5    Spencer, D.6    Higgins, T.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.