메뉴 건너뛰기




Volumn 108, Issue 7, 2004, Pages 1299-1308

Similarities of omega gliadins from Triticum urartu to those encoded on chromosome 1A of hexaploid wheat and evidence for their post-translational processing

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMOSOMES; ELECTROPHORESIS; GENES; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY;

EID: 2442561610     PISSN: 00405752     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00122-003-1565-9     Document Type: Article
Times cited : (50)

References (48)
  • 1
    • 0002977126 scopus 로고    scopus 로고
    • Effect of heat shock during grain filling on the gluten protein composition of bread wheat
    • Ciaffi M, Tozzi L, Borghi B, Corbellini M, Lafiandra D (1996) Effect of heat shock during grain filling on the gluten protein composition of bread wheat. J Cereal Sci 24:91-100
    • (1996) J Cereal Sci , vol.24 , pp. 91-100
    • Ciaffi, M.1    Tozzi, L.2    Borghi, B.3    Corbellini, M.4    Lafiandra, D.5
  • 2
    • 0031019671 scopus 로고    scopus 로고
    • Gliadin polymorphism in wild and cultivated einkorn wheats
    • Ciaffi M, Dominici L, Lafiandra D (1997) Gliadin polymorphism in wild and cultivated einkorn wheats. Theor Appl Genet 94:68-74
    • (1997) Theor Appl Genet , vol.94 , pp. 68-74
    • Ciaffi, M.1    Dominici, L.2    Lafiandra, D.3
  • 4
    • 0033862013 scopus 로고    scopus 로고
    • Effects of temperature and nitrogen nutrition on the grain composition of winter wheat: Effects on gliadin content and composition
    • Daniel C, Triboi E (2000) Effects of temperature and nitrogen nutrition on the grain composition of winter wheat: effects on gliadin content and composition. J Cereal Sci 32:45-56
    • (2000) J Cereal Sci , vol.32 , pp. 45-56
    • Daniel, C.1    Triboi, E.2
  • 5
    • 0000039355 scopus 로고    scopus 로고
    • Efficiency and limitations of immunochemical assays for the testing of gluten-free foods
    • Denery-Papini S, Nicolas Y, Popineau Y (1999) Efficiency and limitations of immunochemical assays for the testing of gluten-free foods. J Cereal Sci 30:121-131
    • (1999) J Cereal Sci , vol.30 , pp. 121-131
    • Denery-Papini, S.1    Nicolas, Y.2    Popineau, Y.3
  • 7
    • 0033800144 scopus 로고    scopus 로고
    • Characterization of the 1B-type omega gliadins from Triticum aestivum 'Butte'
    • DuPont FM, Vensel WH, Chan R, Kasarda DD (2000) Characterization of the 1B-type omega gliadins from Triticum aestivum 'Butte'. Cereal Chem 77:607-614
    • (2000) Cereal Chem , vol.77 , pp. 607-614
    • DuPont, F.M.1    Vensel, W.H.2    Chan, R.3    Kasarda, D.D.4
  • 8
    • 0027272045 scopus 로고
    • The evolution of polyploid wheat: Identification of the A genome donor species
    • Dvorak J, di Terlizzi P, Zhang HB, Resta P (1993) The evolution of polyploid wheat: identification of the A genome donor species. Genome 36:21-31
    • (1993) Genome , vol.36 , pp. 21-31
    • Dvorak, J.1    Di Terlizzi, P.2    Zhang, H.B.3    Resta, P.4
  • 10
    • 0024155242 scopus 로고
    • Primary structure of a C-hordein gene from barley
    • Entwistle J (1988) Primary structure of a C-hordein gene from barley. Carlsberg Res Commun 53:247-258
    • (1988) Carlsberg Res Commun , vol.53 , pp. 247-258
    • Entwistle, J.1
  • 12
    • 0030512422 scopus 로고    scopus 로고
    • Procedure for isolating monomeric proteins and polymeric glutenin of wheat flour
    • Fu BX, Sapirstein HD (1996) Procedure for isolating monomeric proteins and polymeric glutenin of wheat flour. Cereal Chem 73:143-152
    • (1996) Cereal Chem , vol.73 , pp. 143-152
    • Fu, B.X.1    Sapirstein, H.D.2
  • 13
    • 0033799568 scopus 로고    scopus 로고
    • RFLP-based analysis of three RbcS subfamilies in diploid and polypoloid species of wheat
    • Galili G, Avivi Y, Millet E, Feldman M (2000) RFLP-based analysis of three RbcS subfamilies in diploid and polypoloid species of wheat. Mol Gen Genet 263:674-680
    • (2000) Mol Gen Genet , vol.263 , pp. 674-680
    • Galili, G.1    Avivi, Y.2    Millet, E.3    Feldman, M.4
  • 14
    • 0036845735 scopus 로고    scopus 로고
    • Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases
    • Gruis D, Selinger DA, Curran JM, Jung R (2002) Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases. Plant Cell 14:2863-2882
    • (2002) Plant Cell , vol.14 , pp. 2863-2882
    • Gruis, D.1    Selinger, D.A.2    Curran, J.M.3    Jung, R.4
  • 15
    • 0034929179 scopus 로고    scopus 로고
    • Isolation and characterization of wheat ω-gliadin genes
    • Hsia CC, Anderson OD (2001) Isolation and characterization of wheat ω-gliadin genes. Theor Appl Genet 103:37-44
    • (2001) Theor Appl Genet , vol.103 , pp. 37-44
    • Hsia, C.C.1    Anderson, O.D.2
  • 16
    • 0026261706 scopus 로고
    • Isolation and characterisation of genes encoding rye prolamins containing a highly repetitive sequence motif
    • Hull GA, Halford NG, Kreis M, Shewry PR (1991) Isolation and characterisation of genes encoding rye prolamins containing a highly repetitive sequence motif. Plant Mol Biol 17:1111-1115
    • (1991) Plant Mol Biol , vol.17 , pp. 1111-1115
    • Hull, G.A.1    Halford, N.G.2    Kreis, M.3    Shewry, P.R.4
  • 17
    • 0001090938 scopus 로고
    • N-terminal amino acid sequences of ω-gliadins and ω-secalins. Implications for the evolution of prolamin genes
    • Kasarda DD, Autran J-C, Lew EJL, Nimmo CC, Shewry PR (1983) N-terminal amino acid sequences of ω-gliadins and ω-secalins. Implications for the evolution of prolamin genes. Biochim Biophys Acta 747:138-150
    • (1983) Biochim Biophys Acta , vol.747 , pp. 138-150
    • Kasarda, D.D.1    Autran, J.-C.2    Lew, E.J.L.3    Nimmo, C.C.4    Shewry, P.R.5
  • 18
    • 0031937362 scopus 로고    scopus 로고
    • Resolution of high molecular weight glutenin subunits by a new SDS-PAGE system incorporating a neutral pH buffer
    • Kasarda DD, Woodard KM, Adalsteins AE (1998) Resolution of high molecular weight glutenin subunits by a new SDS-PAGE system incorporating a neutral pH buffer. Cereal Chem 75:70-71
    • (1998) Cereal Chem , vol.75 , pp. 70-71
    • Kasarda, D.D.1    Woodard, K.M.2    Adalsteins, A.E.3
  • 19
    • 0000955453 scopus 로고
    • Chromosomal assignment of genes coding for the wheat gliadin protein components of the cultivars 'Cheyenne' and 'Chinese Spring' by two-dimensional (two-pH) electrophoresis
    • Lafiandra D, Kasarda DD, Morris R (1984) Chromosomal assignment of genes coding for the wheat gliadin protein components of the cultivars 'Cheyenne' and 'Chinese Spring' by two-dimensional (two-pH) electrophoresis. Theor Appl Genet 68:531-539
    • (1984) Theor Appl Genet , vol.68 , pp. 531-539
    • Lafiandra, D.1    Kasarda, D.D.2    Morris, R.3
  • 20
    • 0001045321 scopus 로고
    • Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sufate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing
    • Lew EJL, Kuzmicky DD, Kasarda DD(1992) Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sufate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing. Cereal Chem 69:508-515
    • (1992) Cereal Chem , vol.69 , pp. 508-515
    • Lew, E.J.L.1    Kuzmicky, D.D.2    Kasarda, D.D.3
  • 21
    • 0026048007 scopus 로고
    • Two-dimensional electrophoresis of 1D-encoded B and D glutenin subunits in common wheats with similar omega gliadins
    • Masci S, Porceddu E, Lafiandra D (1991) Two-dimensional electrophoresis of 1D-encoded B and D glutenin subunits in common wheats with similar omega gliadins. Biochem Genet 29:403-413
    • (1991) Biochem Genet , vol.29 , pp. 403-413
    • Masci, S.1    Porceddu, E.2    Lafiandra, D.3
  • 22
    • 85010878056 scopus 로고
    • D-glutenin subunits: N-terminal sequences and evidence for the presence of cysteine
    • Masci S, Lafiandra D, Porceddu E, Lew EJ, Tao HP, Kasarda DD (1993) D-glutenin subunits: N-terminal sequences and evidence for the presence of cysteine. Cereal Chem 70:581-585
    • (1993) Cereal Chem , vol.70 , pp. 581-585
    • Masci, S.1    Lafiandra, D.2    Porceddu, E.3    Lew, E.J.4    Tao, H.P.5    Kasarda, D.D.6
  • 23
    • 0032244631 scopus 로고    scopus 로고
    • Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer
    • Masci S, D'Ovidio Lafiandra D, Kasarda DD (1998) Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer. Plant Physiol 118:1147-1158
    • (1998) Plant Physiol , vol.118 , pp. 1147-1158
    • Masci, S.1    D'Ovidio Lafiandra, D.2    Kasarda, D.D.3
  • 24
    • 0036436092 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded ω-type prolamin sequence from wheat
    • Masoudi-Nejad A, Nasuda S, Kawabe A, Endo TR (2002) Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded ω-type prolamin sequence from wheat. Genome 45:661-669
    • (2002) Genome , vol.45 , pp. 661-669
    • Masoudi-Nejad, A.1    Nasuda, S.2    Kawabe, A.3    Endo, T.R.4
  • 25
    • 0346078464 scopus 로고
    • Organization, variability and stability of the family of the gliadin-coding genes in wheat: Genetic data
    • Lasztity R, Békés F (eds) World Scientific, Budapest
    • Metakosky EV, Sozinov AA (1987) Organization, variability and stability of the family of the gliadin-coding genes in wheat: genetic data. In: Lasztity R, Békés F (eds) Proceedings of the 3rd International Workshop on Gluten Proteins. World Scientific, Budapest
    • (1987) Proceedings of the 3rd International Workshop on Gluten Proteins
    • Metakosky, E.V.1    Sozinov, A.A.2
  • 26
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Müntz K, Shutov AD (2002) Legumains and their functions in plants. Trends Plant Sci 8:340-344
    • (2002) Trends Plant Sci , vol.8 , pp. 340-344
    • Müntz, K.1    Shutov, A.D.2
  • 27
    • 0000975155 scopus 로고
    • Genetics of wheat storage proteins and the effect of allelic variation on bread-making quality
    • Payne PI (1987) Genetics of wheat storage proteins and the effect of allelic variation on bread-making quality. Annu Rev Plant Physiol 38:141-153
    • (1987) Annu Rev Plant Physiol , vol.38 , pp. 141-153
    • Payne, P.I.1
  • 28
    • 34250136031 scopus 로고
    • Genetic linkage between endosperm storage protein genes on each of the short arms of chromosomes 1A and 1B in wheat
    • Payne PI, Jackson EA, Holt LM, Law CN (1984) Genetic linkage between endosperm storage protein genes on each of the short arms of chromosomes 1A and 1B in wheat. Theor Appl Genet 67:235-243
    • (1984) Theor Appl Genet , vol.67 , pp. 235-243
    • Payne, P.I.1    Jackson, E.A.2    Holt, L.M.3    Law, C.N.4
  • 29
    • 0026576158 scopus 로고
    • Conformation of wheat gluten proteins. Comparison between functional and solution states as determined by infrared spectroscopy
    • Pézolet M, Bonenfant S, Dousseau F, Popineau Y (1992) Conformation of wheat gluten proteins. Comparison between functional and solution states as determined by infrared spectroscopy. FEBS Lett 299:247-250
    • (1992) FEBS Lett , vol.299 , pp. 247-250
    • Pézolet, M.1    Bonenfant, S.2    Dousseau, F.3    Popineau, Y.4
  • 30
    • 0007733691 scopus 로고
    • Purification and characterization of ω-gliadin components from common wheat
    • Popineau Y, le Guerroue JL, Pineau F (1986) Purification and characterization of ω-gliadin components from common wheat. Lebensm Wiss Technol 19:266-271
    • (1986) Lebensm Wiss Technol , vol.19 , pp. 266-271
    • Popineau, Y.1    Le Guerroue, J.L.2    Pineau, F.3
  • 31
    • 0034925333 scopus 로고    scopus 로고
    • Legumain forms from plants and animals differ in their specificity
    • Rotari VI, Dando PM, Barrett AJ (2001) Legumain forms from plants and animals differ in their specificity. Biol Chem 382:953-959
    • (2001) Biol Chem , vol.382 , pp. 953-959
    • Rotari, V.I.1    Dando, P.M.2    Barrett, A.J.3
  • 32
    • 0001037262 scopus 로고
    • Characterization and organization of gene families at the Gli-1 loci of bread and durum wheats by restriction fragment analysis
    • Sabelli PA, Shewry PR (1991) Characterization and organization of gene families at the Gli-1 loci of bread and durum wheats by restriction fragment analysis. Theor Appl Genet 83:209-216
    • (1991) Theor Appl Genet , vol.83 , pp. 209-216
    • Sabelli, P.A.1    Shewry, P.R.2
  • 33
    • 0001833478 scopus 로고
    • Nullisomic-tetrasomic combinations in hexaploid wheat
    • Lewis DR (ed) Oliver and Boyd, London
    • Sears ER (1954) Nullisomic-tetrasomic combinations in hexaploid wheat. In: Lewis DR (ed) Chromosome manipulation and plant genetics. Oliver and Boyd, London, pp 29-47
    • (1954) Chromosome Manipulation and Plant Genetics , pp. 29-47
    • Sears, E.R.1
  • 34
    • 0000808441 scopus 로고    scopus 로고
    • Comparative investigations of gluten proteins from different wheat species. II. Characterization of omega-gliadins
    • Seilmeier W, Valdez I, Mendez E, Wieser H (2001) Comparative investigations of gluten proteins from different wheat species. II. Characterization of omega-gliadins. Eur Food Res Technol 212:355-363
    • (2001) Eur Food Res Technol , vol.212 , pp. 355-363
    • Seilmeier, W.1    Valdez, I.2    Mendez, E.3    Wieser, H.4
  • 35
    • 0030456404 scopus 로고    scopus 로고
    • Post-translational peptide bond formation during concanavalin a processing in vitro
    • Sheldon PS, Keen JN, Bowles DJ (1996) Post-translational peptide bond formation during concanavalin A processing in vitro. Biochem J 320:865-870
    • (1996) Biochem J , vol.320 , pp. 865-870
    • Sheldon, P.S.1    Keen, J.N.2    Bowles, D.J.3
  • 36
    • 0000952722 scopus 로고
    • N-terminal amino acid sequence homology of storage protein components from barley and a diploid wheat
    • Shewry PR, Autran J-C, Nimmo CC, Lew EJ, Kasarda DD (1981) N-terminal amino acid sequence homology of storage protein components from barley and a diploid wheat. Nature 286:520-522
    • (1981) Nature , vol.286 , pp. 520-522
    • Shewry, P.R.1    Autran, J.-C.2    Nimmo, C.C.3    Lew, E.J.4    Kasarda, D.D.5
  • 37
    • 0035083631 scopus 로고    scopus 로고
    • Chromosomal control of albumins and globulins in wheat grain assessed using different fractionation procedures
    • Singh J, Skerritt J (2001) Chromosomal control of albumins and globulins in wheat grain assessed using different fractionation procedures. J Cereal Sci 33:163-181
    • (2001) J Cereal Sci , vol.33 , pp. 163-181
    • Singh, J.1    Skerritt, J.2
  • 38
    • 0026127867 scopus 로고
    • Enzyme immunoassay for determination of gluten in foods: Collaborative study
    • Skerritt JH, Hill AS (1991) Enzyme immunoassay for determination of gluten in foods: collaborative study. J Assoc Off Anal Chem 74:264
    • (1991) J Assoc off Anal Chem , vol.74 , pp. 264
    • Skerritt, J.H.1    Hill, A.S.2
  • 39
    • 0001211660 scopus 로고
    • The conformation of wheat gluten proteins. The secondary structures and thermal stabilities of α-, β-, gamma-, and omega- Gliadins
    • Tatham AS, Shewry PR (1985) The conformation of wheat gluten proteins. The secondary structures and thermal stabilities of α-, β-, gamma-, and omega- gliadins. J Cereal Sci 3:103-113
    • (1985) J Cereal Sci , vol.3 , pp. 103-113
    • Tatham, A.S.1    Shewry, P.R.2
  • 40
    • 0002470531 scopus 로고
    • The S-poor prolamins of wheat, barley and rye
    • Tatham AS, Shewry PR (1995) The S-poor prolamins of wheat, barley and rye. J Cereal Sci 22:1-16
    • (1995) J Cereal Sci , vol.22 , pp. 1-16
    • Tatham, A.S.1    Shewry, P.R.2
  • 41
    • 0024970049 scopus 로고
    • Conformational studies of a synthetic peptide corresponding to the repeat motif of C-hordein
    • Tatham AS, Drake AF, Shewry PR (1989) Conformational studies of a synthetic peptide corresponding to the repeat motif of C-hordein. Biochem J 259:471-476
    • (1989) Biochem J , vol.259 , pp. 471-476
    • Tatham, A.S.1    Drake, A.F.2    Shewry, P.R.3
  • 42
    • 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
    • Thomson NH, Miles MJ, Popineau Y, Harries J, Shewry PR, Tatham AS (1999) 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 1430:359-366
    • (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.R.5    Tatham, A.S.6
  • 43
    • 84985321904 scopus 로고
    • The baking quality and protein characteristics of a winter wheat grown at different levels of nitrogen fertilisation
    • Timms MF, Bottomley RC, Ellis JRS, Schofield JD (1981) The baking quality and protein characteristics of a winter wheat grown at different levels of nitrogen fertilisation. J Sci Food Agric 32:684-698
    • (1981) J Sci Food Agric , vol.32 , pp. 684-698
    • Timms, M.F.1    Bottomley, R.C.2    Ellis, J.R.S.3    Schofield, J.D.4
  • 44
    • 0002034788 scopus 로고
    • Electrophoretic analysis of the high-molecular-weight glutenin subunits of Triticum monococcum, T. urartu, and the a genome of bread wheat (T. aestivum)
    • Waines JG, Payne PI (1987) Electrophoretic analysis of the high-molecular-weight glutenin subunits of Triticum monococcum, T. urartu, and the A genome of bread wheat (T. aestivum). Theor Appl Genet 74:71-76
    • (1987) Theor Appl Genet , vol.74 , pp. 71-76
    • Waines, J.G.1    Payne, P.I.2
  • 45
    • 0029952769 scopus 로고    scopus 로고
    • Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of omega-gliadins
    • Wellner N, Belton PS, Tatham AS (1996) Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of omega-gliadins. Biochem J 319:741-747
    • (1996) Biochem J , vol.319 , pp. 741-747
    • Wellner, N.1    Belton, P.S.2    Tatham, A.S.3
  • 46
    • 0002344498 scopus 로고    scopus 로고
    • The influence of nitrogen fertilization on quantities and proportions of different protein types in wheat flour
    • Wieser H, Seilmeier W (1998) The influence of nitrogen fertilization on quantities and proportions of different protein types in wheat flour. J Sci Food Agric 76:49-55
    • (1998) J Sci Food Agric , vol.76 , pp. 49-55
    • Wieser, H.1    Seilmeier, W.2
  • 47
    • 0015690724 scopus 로고
    • Electrofocusing of grain proteins from wheat genotypes
    • Wrigley CW, Shepherd KW (1973) Electrofocusing of grain proteins from wheat genotypes. Ann NY Acad Sci 209:154-162
    • (1973) Ann NY Acad Sci , vol.209 , pp. 154-162
    • Wrigley, C.W.1    Shepherd, K.W.2
  • 48
    • 0002120511 scopus 로고
    • Changes in polypeptide composition and grain quality due to sulfur deficiency in wheat
    • Wrigley CW, Du Cros DL, Fullington JG, Kasarda DD (1984) Changes in polypeptide composition and grain quality due to sulfur deficiency in wheat. J Cereal Sci 2:15-24
    • (1984) J Cereal Sci , vol.2 , pp. 15-24
    • Wrigley, C.W.1    Du Cros, D.L.2    Fullington, J.G.3    Kasarda, D.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.