메뉴 건너뛰기




Volumn 46, Issue 2, 2006, Pages 358-366

Cloning, bacterial expression, purification and structural characterization of N-terminal-repetitive domain of γ-Gliadin

Author keywords

Gliadin; Circular dichroism; Repetitive domain; Thioredoxin; Wheat storage proteins

Indexed keywords

GLIADIN; HYBRID PROTEIN;

EID: 33645419299     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.08.017     Document Type: Article
Times cited : (5)

References (54)
  • 1
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: Structures, properties and role in grain utilization
    • P.R. Shewry, and N. Halford Cereal seed storage proteins: structures, properties and role in grain utilization J. Exp. Bot. 53 2002 947 958
    • (2002) J. Exp. Bot. , vol.53 , pp. 947-958
    • Shewry, P.R.1    Halford, N.2
  • 2
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • P.R. Shewry, and A.S. Tatham The prolamin storage proteins of cereal seeds: structure and evolution Biochem. J. 267 1990 1 12
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 4
    • 0037208926 scopus 로고    scopus 로고
    • The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties
    • P.R. Shewry, N. Halford, A.S. Tatham, Y. Popineau, D. Lafiandra, and P.S. Belton The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties Adv. Food Nutr. Res. 45 2003 219 302
    • (2003) Adv. Food Nutr. Res. , vol.45 , pp. 219-302
    • Shewry, P.R.1    Halford, N.2    Tatham, A.S.3    Popineau, Y.4    Lafiandra, D.5    Belton, P.S.6
  • 5
    • 0035943660 scopus 로고    scopus 로고
    • Role of individual disulfide bonds in the structural maturation of a low molecular weight glutenin subunit
    • A. Orsi, F. Sparvoli, and A. Ceriotti Role of individual disulfide bonds in the structural maturation of a low molecular weight glutenin subunit J. Biol. Chem. 276 2001 32322 32329
    • (2001) J. Biol. Chem. , vol.276 , pp. 32322-32329
    • Orsi, A.1    Sparvoli, F.2    Ceriotti, A.3
  • 6
    • 0001920021 scopus 로고    scopus 로고
    • Mini review: On the elasticity of wheat gluten
    • P.S. Belton Mini review: on the elasticity of wheat gluten J. Cereal Sci. 29 1999 103 107
    • (1999) J. Cereal Sci. , vol.29 , pp. 103-107
    • Belton, P.S.1
  • 7
    • 0042342289 scopus 로고    scopus 로고
    • Coeliac disease
    • M. Mäki, and P. Collin Coeliac disease Lancet 349 1997 1755 1759
    • (1997) Lancet , vol.349 , pp. 1755-1759
    • Mäki, M.1    Collin, P.2
  • 8
    • 0028985359 scopus 로고
    • Characterization of distinct a- and g-type gliadins and low molecular weight components from wheat endosperm as coeliac immunoreactive proteins
    • A. Rocher, F. Soriano, E. Molina, G. González-Limas, and E. Méndez Characterization of distinct a- and g-type gliadins and low molecular weight components from wheat endosperm as coeliac immunoreactive proteins Biochim. Biophys. Acta 1247 1995 143 148
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 143-148
    • Rocher, A.1    Soriano, F.2    Molina, E.3    González-Limas, G.4    Méndez, E.5
  • 9
    • 0037486873 scopus 로고    scopus 로고
    • Food allergy to wheat: Identification of immunogloglin e and immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour
    • F. Battais, F. Pineau, Y. Popineau, C. Aparicio, G. Kanny, L. Guerin, D.A. Moneret-Vautrin, and S. Denery-Papini Food allergy to wheat: identification of immunogloglin E and immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour Clin. Exp. Allergy 33 2003 962 970
    • (2003) Clin. Exp. Allergy , vol.33 , pp. 962-970
    • Battais, F.1    Pineau, F.2    Popineau, Y.3    Aparicio, C.4    Kanny, G.5    Guerin, L.6    Moneret-Vautrin, D.A.7    Denery-Papini, S.8
  • 10
  • 11
    • 0034066695 scopus 로고    scopus 로고
    • In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope
    • R.P. Anderson, P. Degano, A.J. Godkin, D. Jewell, and A.V.S. Hill In vivo antigen challenge in celiac disease identifies a single transglutaminase- modified peptide as the dominant A-gliadin T-cell epitope Nat. Med. 6 2000 337 342
    • (2000) Nat. Med. , vol.6 , pp. 337-342
    • Anderson, R.P.1    Degano, P.2    Godkin, A.J.3    Jewell, D.4    Hill, A.V.S.5
  • 13
    • 0034075469 scopus 로고    scopus 로고
    • Production of a panel of recombinant gliadins for the characterisation of T cell reactivity in coeliac disease
    • E.H. Arentz-Hansen, S.N. McAdam, Ø Molberg, C. Kristiansen, and L.M. Sollid Production of a panel of recombinant gliadins for the characterisation of T cell reactivity in coeliac disease Gut 46 2000 46 51
    • (2000) Gut , vol.46 , pp. 46-51
    • Arentz-Hansen, E.H.1    McAdam, S.N.2    Molberg Ø3    Kristiansen, C.4    Sollid, L.M.5
  • 14
    • 33645412822 scopus 로고    scopus 로고
    • Coeliac disease-specific toxicological and immunological studies of peptides from α-gliadins
    • D. Lafiandra, S. Masci, R. D'Ovidio (Eds). RSC
    • H. Wieser, W. Engel, J. Fraser, E. Pollock, H.J. Ellis, P.J. Ciclitira, Coeliac disease-specific toxicological and immunological studies of peptides from α-gliadins. in: D. Lafiandra, S. Masci, R. D'Ovidio (Eds). The Gluten Proteins. RSC (2004) 371-378.
    • (2004) The Gluten Proteins , pp. 371-378
    • Wieser, H.1    Engel, W.2    Fraser, J.3    Pollock, E.4    Ellis, H.J.5    Ciclitira, P.J.6
  • 15
  • 18
    • 0001211660 scopus 로고
    • The conformation of wheat gluten proteins the secondary structure and thermal stabilities of α-, β-, γ-, and ω-gliadins
    • A.S. Tatham, and P.R. Shewry The conformation of wheat gluten proteins The secondary structure and thermal stabilities of α-, β-, γ-, and ω-gliadins J. Cereal Sci. 3 1985 103 113
    • (1985) J. Cereal Sci. , vol.3 , pp. 103-113
    • Tatham, A.S.1    Shewry, P.R.2
  • 19
    • 0002191984 scopus 로고
    • Secondary structures of wheat α- And ω-gliadin proteins: Fourier transform Infrared spectroscopy
    • J.M. Purcell, D.D. Kasarda, and C.S. Wu Secondary structures of wheat α- and ω-gliadin proteins: Fourier transform Infrared spectroscopy J. Cereal Sci. 7 1988 21 32
    • (1988) J. Cereal Sci. , vol.7 , pp. 21-32
    • Purcell, J.M.1    Kasarda, D.D.2    Wu, C.S.3
  • 21
    • 0032985443 scopus 로고    scopus 로고
    • Small angle X ray scattering of wheat seed-storage proteins: α-, γ-, and ω-gliadins and the high molecular weight (HMW) subunits of glutenin
    • N.H. Thomson, M.J. Miles, Y. Popineau, J. Harries, P. Shewry, and A.S. Tatham Small angle X ray scattering of wheat seed-storage proteins: α-, γ-, and ω-gliadins and the high molecular weight (HMW) subunits of glutenin Biochim. Biophys. Acta 1430 1999 359 366
    • (1999) Biochim. Biophys. Acta , vol.1430 , pp. 359-366
    • Thomson, N.H.1    Miles, M.J.2    Popineau, Y.3    Harries, J.4    Shewry, P.5    Tatham, A.S.6
  • 23
    • 0002436112 scopus 로고
    • Conformational studies of peptides derived by the enzymatic hydrolysis of a γ-Gliadin
    • A.S. Tatham, P. Masson, and Y. Popineau Conformational studies of peptides derived by the enzymatic hydrolysis of a γ-Gliadin J. Cereal Sci. 11 1990 1 13
    • (1990) J. Cereal Sci. , vol.11 , pp. 1-13
    • Tatham, A.S.1    Masson, P.2    Popineau, Y.3
  • 24
    • 0030603249 scopus 로고    scopus 로고
    • Construction and expression of a synthetic wheat storage protein gene
    • O.D. Anderson, J.C. Kuhl, and A. Tam Construction and expression of a synthetic wheat storage protein gene Gene 174 1996 51 58
    • (1996) Gene , vol.174 , pp. 51-58
    • Anderson, O.D.1    Kuhl, J.C.2    Tam, A.3
  • 25
    • 0030972492 scopus 로고    scopus 로고
    • Structure characterisation of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state
    • A.A. van Dijk, E. de Boef, A. Bekkers, L.L. van Wijk, E. van Swieten, R.J. Hamer, and G.T. Robillard Structure characterisation of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state Protein Sci. 6 1997 649 656
    • (1997) Protein Sci. , vol.6 , pp. 649-656
    • Van Dijk, A.A.1    De Boef, E.2    Bekkers, A.3    Van Wijk, L.L.4    Van Swieten, E.5    Hamer, R.J.6    Robillard, G.T.7
  • 26
    • 0000486642 scopus 로고    scopus 로고
    • Physical characterisation of the N-terminal domain of high molecular weight glutenin subunit Dx5 from wheat
    • A.A. van Dijk, E. van Swieten, I.T. Kruize, and G.T. Robillard Physical characterisation of the N-terminal domain of high molecular weight glutenin subunit Dx5 from wheat J. Cereal Sci. 28 1998 115 126
    • (1998) J. Cereal Sci. , vol.28 , pp. 115-126
    • Van Dijk, A.A.1    Van Swieten, E.2    Kruize, I.T.3    Robillard, G.T.4
  • 30
    • 0035820397 scopus 로고    scopus 로고
    • Synthesis, expression and characterisation of peptides comprised of perfect repeat motifs based on a wheat storage protein
    • K.A. Feeney, A.S. Tatham, S.M. Gilbert, R.J. Fdo, N.G. Halford, and P.R. Shewry Synthesis, expression and characterisation of peptides comprised of perfect repeat motifs based on a wheat storage protein Biochim. Biophys. Acta 1546 2001 346 355
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 346-355
    • Feeney, K.A.1    Tatham, A.S.2    Gilbert, S.M.3    Fdo, R.J.4    Halford, N.G.5    Shewry, P.R.6
  • 32
    • 0037465679 scopus 로고    scopus 로고
    • Heterologous expression and purification of native and mutated low molecular mass glutenin subunits from durum wheat
    • C. Patacchini, S. Masci, R. D'Ovidio, and D. Lafiandra Heterologous expression and purification of native and mutated low molecular mass glutenin subunits from durum wheat J. Chromatogr. B 786 2003 215 220
    • (2003) J. Chromatogr. B , vol.786 , pp. 215-220
    • Patacchini, C.1    Masci, S.2    D'Ovidio, R.3    Lafiandra, D.4
  • 33
    • 0037931535 scopus 로고    scopus 로고
    • Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. I small-angle neutron scattering
    • S.U. Egelhaaf, E. van Swieten, T. Bosma, E. de Boef, A.A. van Dijk, and G.T. Robillard Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. I small-angle neutron scattering Biopolymers 69 2003 311 324
    • (2003) Biopolymers , vol.69 , pp. 311-324
    • Egelhaaf, S.U.1    Van Swieten, E.2    Bosma, T.3    De Boef, E.4    Van Dijk, A.A.5    Robillard, G.T.6
  • 34
    • 0038268813 scopus 로고    scopus 로고
    • Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. II Hydrodynamic studies
    • E. van Swieten, R.R. Friesen, C.G. de Kruif, and G.T. Robillard Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. II Hydrodynamic studies Biopolymers 69 2003 325 332
    • (2003) Biopolymers , vol.69 , pp. 325-332
    • Van Swieten, E.1    Friesen, R.R.2    De Kruif, C.G.3    Robillard, G.T.4
  • 35
    • 0031561440 scopus 로고    scopus 로고
    • Synthetic genes specifying periodic polymers modelled on the repetitive domain of wheat gliadins: Conception and expression
    • K. Elmorjani, M. Thievin, T. Michon, Y. Popineau, J.N. Hallet, and J. Guéguen Synthetic genes specifying periodic polymers modelled on the repetitive domain of wheat gliadins: conception and expression Biochem. Biophys. Res. Commun. 239 1997 240 246
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 240-246
    • Elmorjani, K.1    Thievin, M.2    Michon, T.3    Popineau, Y.4    Hallet, J.N.5    Guéguen, J.6
  • 36
    • 0344495386 scopus 로고    scopus 로고
    • High microbial production and characterization of strictly periodic polymers modelled on the repetitive domain of wheat gliadins
    • S. Sourice, A. Nisole, J. Guéguen, Y. Popineau, and K. Elmorjani High microbial production and characterization of strictly periodic polymers modelled on the repetitive domain of wheat gliadins Bochim. Biophys. Res. Commun. 312 2003 989 996
    • (2003) Bochim. Biophys. Res. Commun. , vol.312 , pp. 989-996
    • Sourice, S.1    Nisole, A.2    Guéguen, J.3    Popineau, Y.4    Elmorjani, K.5
  • 37
    • 0023081320 scopus 로고
    • Expression of a wheat α gliadin gene in Saccharomyces cerevisiae
    • J.D. Neill, J.C. Litts, O.D. Anderson, F.C. Greene, and J.I. Stiles Expression of a wheat α gliadin gene in Saccharomyces cerevisiae Gene 55 1987 303 317
    • (1987) Gene , vol.55 , pp. 303-317
    • Neill, J.D.1    Litts, J.C.2    Anderson, O.D.3    Greene, F.C.4    Stiles, J.I.5
  • 38
    • 0000293328 scopus 로고
    • Expression of a wheat gliadin protein in yeast (Saccharomyces cerevisiae)
    • K.A. Pratt, P.J. Madwick, and P.R. Shewry Expression of a wheat gliadin protein in yeast (Saccharomyces cerevisiae) J. Cereal Sci. 14 1991 223 229
    • (1991) J. Cereal Sci. , vol.14 , pp. 223-229
    • Pratt, K.A.1    Madwick, P.J.2    Shewry, P.R.3
  • 39
    • 0343350512 scopus 로고
    • Wheat Tritucum aestivum γ-gliadin accumulates in dense protein bodies within the endoplasmic reticulum of yeast
    • N. Rosenberg, Y. Shimoni, Y. Altschuler, H. Levanony, M. Volokita, and G. Galili Wheat Tritucum aestivum γ-gliadin accumulates in dense protein bodies within the endoplasmic reticulum of yeast Plant physiol. 102 1993 67 69
    • (1993) Plant Physiol. , vol.102 , pp. 67-69
    • Rosenberg, N.1    Shimoni, Y.2    Altschuler, Y.3    Levanony, H.4    Volokita, M.5    Galili, G.6
  • 40
    • 0028248853 scopus 로고
    • Two structural domains mediate two sequential events in γ-zein targeting protein endoplasmic reticulum retention and protein body formation
    • M.I. Geli, M. Torrent, and D. Ludevid Two structural domains mediate two sequential events in γ-zein targeting protein endoplasmic reticulum retention and protein body formation Plant Cell 6 1994 1911 1922
    • (1994) Plant Cell , vol.6 , pp. 1911-1922
    • Geli, M.I.1    Torrent, M.2    Ludevid, D.3
  • 41
    • 0029736859 scopus 로고    scopus 로고
    • Integration and expression of the high-molecular-weight glutenin subunit 1Ax1 gene into wheat
    • F. Alpeter, V. Vasil, V. Srivastava, and I.K. Vasil Integration and expression of the high-molecular-weight glutenin subunit 1Ax1 gene into wheat Nat. Biotechnol. 14 1996 1155 1159
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1155-1159
    • Alpeter, F.1    Vasil, V.2    Srivastava, V.3    Vasil, I.K.4
  • 42
    • 0030339563 scopus 로고    scopus 로고
    • The maize γ-zein sequesters a-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm
    • C.E. Coleman, E.M. Herman, K. Takasaki, and B.A. Larkins The maize γ-zein sequesters a-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
  • 44
    • 0034645802 scopus 로고    scopus 로고
    • A modified 10 kDa zein protein, produces two morphologically distinct protein bodies in transgenic tobacco
    • J. Randall, S. Bagga, H. Adams, and J. Kemp A modified 10 kDa zein protein, produces two morphologically distinct protein bodies in transgenic 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.4
  • 46
    • 0028222351 scopus 로고
    • Role of conserved cisteines of a wheat gliadin in its transport and assembly into protein bodies in Xenopus oocytes
    • Y. Altschuler, and G. Galili Role of conserved cisteines of a wheat gliadin in its transport and assembly into protein bodies in Xenopus oocytes J. Biol. Chem. 269 1994 6677 6682
    • (1994) J. Biol. Chem. , vol.269 , pp. 6677-6682
    • Altschuler, Y.1    Galili, G.2
  • 47
  • 48
    • 0001639807 scopus 로고
    • Molecular analysis of γ-gliadin gene families at the complex Gli-1 locus of bread wheat (T. aestivum L.)
    • D. Bartels, I. Altosaar, N.P. Harberd, Barker, and R.D. Thompson Molecular analysis of γ-gliadin gene families at the complex Gli-1 locus of bread wheat (T. aestivum L.) Theor. Appl. Genet. 72 1986 845 853
    • (1986) Theor. Appl. Genet. , vol.72 , pp. 845-853
    • Bartels, D.1    Altosaar, I.2    Harberd, N.P.3    Barker4    Thompson, R.D.5
  • 50
    • 33746977587 scopus 로고
    • Variation in estimates of molecular weight of cereal prolamins by SDS-AGE
    • N. Bunce, R.P. White, and P.R. Shewry Variation in estimates of molecular weight of cereal prolamins by SDS-AGE J. Cereal Sci. 3 1985 111 142
    • (1985) J. Cereal Sci. , vol.3 , pp. 111-142
    • Bunce, N.1    White, R.P.2    Shewry, P.R.3
  • 51
    • 0006541289 scopus 로고
    • Changes of conformation and surface hydrohobicity of gliadins
    • Y. Popineau, and F. Pineau Changes of conformation and surface hydrohobicity of gliadins Lebensm-Wiss. u.-Technol. 21 1988 113 117
    • (1988) Lebensm-Wiss. U.-Technol. , vol.21 , pp. 113-117
    • Popineau, Y.1    Pineau, F.2
  • 52
    • 0001591391 scopus 로고    scopus 로고
    • The central domain of high molecular weight glutenin dubunits is water-soluble
    • A.C.A.P.A. Bekkers, E. de Boef, A.A. van Dijk, and R.J. Hamer The central domain of high molecular weight glutenin dubunits is water-soluble J. Cereal Sci. 29 1999 109 112
    • (1999) J. Cereal Sci. , vol.29 , pp. 109-112
    • Bekkers, A.C.A.P.A.1    De Boef, E.2    Van Dijk, A.A.3    Hamer, R.J.4
  • 53
    • 0345578674 scopus 로고    scopus 로고
    • Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length
    • K.A. Feeney, N. Wellner, S.M. Gilbert, N.G. Halford, A.S. Tatham, P.R. Shewry, and P.S. Belton Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length Biopolymers 72 2003 123 131
    • (2003) Biopolymers , vol.72 , pp. 123-131
    • Feeney, K.A.1    Wellner, N.2    Gilbert, S.M.3    Halford, N.G.4    Tatham, A.S.5    Shewry, P.R.6    Belton, P.S.7
  • 54
    • 33645415298 scopus 로고    scopus 로고
    • Use of recombinant polypeptides to explore the mechanism of gluten protein viscoelasticity
    • D. Lafiandra, S. Masci, R. D'Ovidio (Eds). RSC
    • N.G. Halford, A. Savage, N. Wellner, E.N.C. Mills, P.S. Belton, P.R. Shewry, Use of recombinant polypeptides to explore the mechanism of gluten protein viscoelasticity. in: D. Lafiandra, S. Masci, R. D'Ovidio (Eds). The Gluten Proteins. RSC (2004) 54-57.
    • (2004) The Gluten Proteins , pp. 54-57
    • Halford, N.G.1    Savage, A.2    Wellner, N.3    Mills, E.N.C.4    Belton, P.S.5    Shewry, P.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.