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Volumn 170, Issue 4, 2006, Pages 808-821

Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome

Author keywords

1,3 Endoglucanase; 1 Cys peroxiredoxin; 2D gel electrophoresis; Barley cultivars; Mass spectrometry; Protein isoforms

Indexed keywords

CROPS; CULTIVATION; MASS SPECTROMETRY;

EID: 32644485468     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2005.11.012     Document Type: Article
Times cited : (57)

References (44)
  • 1
    • 0026519178 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis, with immobilized pH gradients in the first dimension, of barley seed proteins: Discrimination of cultivars with different malting grades
    • A. Görg, W. Postel, M. Baumer, and W. Weiss Two-dimensional polyacrylamide gel electrophoresis, with immobilized pH gradients in the first dimension, of barley seed proteins: discrimination of cultivars with different malting grades Electrophoresis 13 1992 192 203
    • (1992) Electrophoresis , vol.13 , pp. 192-203
    • Görg, A.1    Postel, W.2    Baumer, M.3    Weiss, W.4
  • 3
    • 0035983666 scopus 로고    scopus 로고
    • Proteomics of Arabidopsis seed germination. a comparative study of wild-type and gibberellin-deficient seeds
    • K. Gallardo, C. Job, S.P. Groot, M. Puype, H. Demol, J. Vandekerckhove, and D. Job Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds Plant Physiol. 129 2002 823 837
    • (2002) Plant Physiol. , vol.129 , pp. 823-837
    • Gallardo, K.1    Job, C.2    Groot, S.P.3    Puype, M.4    Demol, H.5    Vandekerckhove, J.6    Job, D.7
  • 5
    • 0035654851 scopus 로고    scopus 로고
    • The wheat-grain proteome as a basis for more efficient cultivar identification
    • D.J. Skylas, L. Copeland, W.G. Rathmell, and C.W. Wrigley The wheat-grain proteome as a basis for more efficient cultivar identification Proteomics 1 2001 1542 1546
    • (2001) Proteomics , vol.1 , pp. 1542-1546
    • Skylas, D.J.1    Copeland, L.2    Rathmell, W.G.3    Wrigley, C.W.4
  • 10
    • 0037953141 scopus 로고    scopus 로고
    • Feasibility study of a tissue-specific approach to barley proteome analysis: Aleurone layer, endosperm, embryo and single seeds
    • C. Finnie, and B. Svensson Feasibility study of a tissue-specific approach to barley proteome analysis: aleurone layer, endosperm, embryo and single seeds J. Cereal Sci. 38 2003 217 226
    • (2003) J. Cereal Sci. , vol.38 , pp. 217-226
    • Finnie, C.1    Svensson, B.2
  • 11
    • 1542615443 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis pattern (pI 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry
    • K.S. Bak-Jensen, S. Laugesen, P. Roepstorff, and B. Svensson Two-dimensional electrophoresis pattern (pI 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry Proteomics 4 2004 728 742
    • (2004) Proteomics , vol.4 , pp. 728-742
    • Bak-Jensen, K.S.1    Laugesen, S.2    Roepstorff, P.3    Svensson, B.4
  • 12
    • 3543141896 scopus 로고    scopus 로고
    • Proteome analysis of barley seeds: Identification of major proteins from two-dimensional gels (pI 4-7)
    • O. Østergaard, C. Finnie, S. Laugesen, P. Roepstorff, and B. Svensson Proteome analysis of barley seeds: identification of major proteins from two-dimensional gels (pI 4-7) Proteomics 4 2004 2437 2447
    • (2004) Proteomics , vol.4 , pp. 2437-2447
    • Østergaard, O.1    Finnie, C.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 13
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome
    • K. Maeda, C. Finnie, O. Østergaard, and B. Svensson Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome Eur. J. Biochem. 270 2003 2633 2643
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Østergaard, O.3    Svensson, B.4
  • 14
    • 1642409412 scopus 로고    scopus 로고
    • Cy5 maleimide-labelling for sensitive detection of free thiols in native protein extracts: Identification of seed proteins targeted by barley thioredoxin h isoforms
    • K. Maeda, C. Finnie, and B. Svensson Cy5 maleimide-labelling for sensitive detection of free thiols in native protein extracts: identification of seed proteins targeted by barley thioredoxin h isoforms Biochem. J. 378 2004 497 507
    • (2004) Biochem. J. , vol.378 , pp. 497-507
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 15
    • 17844411493 scopus 로고    scopus 로고
    • Differential labelling of cysteines for simultaneous identification of thioredoxin h-reducible disulphides in native protein extracts: Insight into recognition and regulation of proteins in barley seeds by thioredoxin h
    • K. Maeda, C. Finnie, and B. Svensson Differential labelling of cysteines for simultaneous identification of thioredoxin h-reducible disulphides in native protein extracts: insight into recognition and regulation of proteins in barley seeds by thioredoxin h Proteomics 5 2005 1634 1644
    • (2005) Proteomics , vol.5 , pp. 1634-1644
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 16
    • 0035983965 scopus 로고    scopus 로고
    • Proteome analysis of grain filling and seed maturation in barley
    • C. Finnie, S. Melchior, P. Roepstorff, and B. Svensson Proteome analysis of grain filling and seed maturation in barley Plant Physiol. 129 2002 1308 1319
    • (2002) Plant Physiol. , vol.129 , pp. 1308-1319
    • Finnie, C.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 17
    • 84981809484 scopus 로고
    • A decimal code for the growth stages of cereals
    • J.C. Zadoks, T.T. Chang, and C.F. Konzak A decimal code for the growth stages of cereals Weed Res. 14 1974 415 421
    • (1974) Weed Res. , vol.14 , pp. 415-421
    • Zadoks, J.C.1    Chang, T.T.2    Konzak, C.F.3
  • 18
    • 0037114993 scopus 로고    scopus 로고
    • Proteolysis during the isoelectric focussing step of 2-dimensional gel electrophoresis may be a common problem
    • C. Finnie, and B. Svensson Proteolysis during the isoelectric focussing step of 2-dimensional gel electrophoresis may be a common problem Anal. Biochem. 311 2002 182 186
    • (2002) Anal. Biochem. , vol.311 , pp. 182-186
    • Finnie, C.1    Svensson, B.2
  • 19
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • J. Heukeshoven, and R. Dernick Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels Electrophoresis 9 1988 28 32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • J. Gobom, E. Nordhoff, E. Mirgorodskaya, R. Ekman, and P. Roepstorff Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry J. Mass Spectrom. 34 1999 105 116
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 23
    • 1342311966 scopus 로고    scopus 로고
    • Transcript profiles and deduced changes of metabolic pathways in maternal and filial tissues of developing barley grains
    • N. Sreenivasulu, L. Altschmied, V. Radchuk, S. Gubatz, U. Wobus, and W. Weschke Transcript profiles and deduced changes of metabolic pathways in maternal and filial tissues of developing barley grains Plant J. 37 2004 539 553
    • (2004) Plant J. , vol.37 , pp. 539-553
    • Sreenivasulu, N.1    Altschmied, L.2    Radchuk, V.3    Gubatz, S.4    Wobus, U.5    Weschke, W.6
  • 24
    • 0028518845 scopus 로고
    • Dehydration and ABA increase messenger-RNA levels and enzyme-activity of cytosolic GAPDH in the resurrection plant Craterostigma-plantagineum
    • R. Velasco, F. Salamini, and D. Bartels Dehydration and ABA increase messenger-RNA levels and enzyme-activity of cytosolic GAPDH in the resurrection plant Craterostigma-plantagineum Plant Mol. Biol. 26 1994 541 546
    • (1994) Plant Mol. Biol. , vol.26 , pp. 541-546
    • Velasco, R.1    Salamini, F.2    Bartels, D.3
  • 25
    • 0030878727 scopus 로고    scopus 로고
    • Water-stress response in Aspen (Populus tremula): Differential accumulation of dehydrin, sucrose synthase, GAPDH homologues, and soluble sugars
    • D. Pelah, O. Shoseyov, A. Altman, and D. Bartels Water-stress response in Aspen (Populus tremula): differential accumulation of dehydrin, sucrose synthase, GAPDH homologues, and soluble sugars J. Plant Physiol. 151 1997 96 100
    • (1997) J. Plant Physiol. , vol.151 , pp. 96-100
    • Pelah, D.1    Shoseyov, O.2    Altman, A.3    Bartels, D.4
  • 26
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • J. Kim, and C.V. Dang Multifaceted roles of glycolytic enzymes Trends Biochem. Sci. 30 2005 142 150
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 142-150
    • Kim, J.1    Dang, C.V.2
  • 27
    • 0027208778 scopus 로고
    • Arginine is essential for the alpha-amylase inhibitory activity of the alpha-amylase/subtilisin inhibitor (BASI) from barley-seeds
    • J. Abe, U. Sidenius, and B. Svensson Arginine is essential for the alpha-amylase inhibitory activity of the alpha-amylase/subtilisin inhibitor (BASI) from barley-seeds Biochem. J. 293 1993 151 155
    • (1993) Biochem. J. , vol.293 , pp. 151-155
    • Abe, J.1    Sidenius, U.2    Svensson, B.3
  • 29
    • 0036164521 scopus 로고    scopus 로고
    • Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases - Structure, function and potential for crop protection
    • O.L. Franco, D.J. Rigden, F.R. Melo, and M.F. Grossi-De-Sa Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases - Structure, function and potential for crop protection Eur. J. Biochem. 269 2002 397 412
    • (2002) Eur. J. Biochem. , vol.269 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi-De-Sa, M.F.4
  • 30
    • 0034004638 scopus 로고    scopus 로고
    • The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance
    • N. Wehmeyer, and E. Vierling The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance Plant Physiol. 122 2000 1099 1108
    • (2000) Plant Physiol. , vol.122 , pp. 1099-1108
    • Wehmeyer, N.1    Vierling, E.2
  • 31
    • 0034930660 scopus 로고    scopus 로고
    • Changes in oligosaccharide content and antioxidant enzyme activities in developing bean seeds as related to acquisition of drying tolerance and seed quality
    • C. Bailly, C. Audigier, F. Ladonne, M.H. Wagner, F. Coste, F. Corbineau, and D. Côme Changes in oligosaccharide content and antioxidant enzyme activities in developing bean seeds as related to acquisition of drying tolerance and seed quality J. Exp. Bot. 52 2001 701 708
    • (2001) J. Exp. Bot. , vol.52 , pp. 701-708
    • Bailly, C.1    Audigier, C.2    Ladonne, F.3    Wagner, M.H.4    Coste, F.5    Corbineau, F.6    Côme, D.7
  • 33
    • 0030237516 scopus 로고    scopus 로고
    • A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains
    • R.A. Stacy, E. Munthe, T. Steinum, B. Sharma, and R.B. Aalen A peroxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains Plant Mol. Biol. 31 1996 1205 1216
    • (1996) Plant Mol. Biol. , vol.31 , pp. 1205-1216
    • Stacy, R.A.1    Munthe, E.2    Steinum, T.3    Sharma, B.4    Aalen, R.B.5
  • 34
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • T. Rabilloud, M. Heller, F. Gasnier, S. Luche, C. Rey, R. Aebersold, M. Benahmed, P. Louisot, and J. Lunardi Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site J. Biol. Chem. 277 2002 19396 19401
    • (2002) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 36
    • 0037106326 scopus 로고    scopus 로고
    • A method for dewtection of overoxidation of cysteines: Peroxiredoxins are oxidised in vivo at the active site cysteine during oxidative stress
    • E. Wagner, S. Luche, L. Penna, M. Chevallet, A. Van Dorsselaer, E. Leize-Wagner, and T. Rabilloud A method for dewtection of overoxidation of cysteines: peroxiredoxins are oxidised in vivo at the active site cysteine during oxidative stress Biochem. J. 366 2002 777 785
    • (2002) Biochem. J. , vol.366 , pp. 777-785
    • Wagner, E.1    Luche, S.2    Penna, L.3    Chevallet, M.4    Van Dorsselaer, A.5    Leize-Wagner, E.6    Rabilloud, T.7
  • 37
    • 0026063521 scopus 로고
    • Biochemical and molecular characterisation of three barley seed proteins with antifungal properties
    • R. Leah, H. Tommerup, I. Svendsen, and J. Mundy Biochemical and molecular characterisation of three barley seed proteins with antifungal properties J. Biol. Chem. 266 1991 1564 1573
    • (1991) J. Biol. Chem. , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 38
    • 0032557916 scopus 로고    scopus 로고
    • Gene structure and a possible cytoplasmic location for (1 → 3)-beta-glucanase isoenzyme GI from barley (Hordeum vulgare)
    • R.A. Burton, Z.W. Qi, S. Roulin, and G.B. Fincher Gene structure and a possible cytoplasmic location for (1 → 3)-beta-glucanase isoenzyme GI from barley (Hordeum vulgare) Plant Sci. 135 1998 39 47
    • (1998) Plant Sci. , vol.135 , pp. 39-47
    • Burton, R.A.1    Qi, Z.W.2    Roulin, S.3    Fincher, G.B.4
  • 40
    • 0030833653 scopus 로고    scopus 로고
    • Cell wall (1-3)- and (1-3, 1-4)-β-glucans during early grain development in rice (Oryza sativa L.)
    • R.C. Brown, B.E. Lemmon, B.A. Stone, and O.-A. Olsen Cell wall (1-3)- and (1-3, 1-4)-β-glucans during early grain development in rice (Oryza sativa L.) Planta 202 1997 414 426
    • (1997) Planta , vol.202 , pp. 414-426
    • Brown, R.C.1    Lemmon, B.E.2    Stone, B.A.3    Olsen, O.-A.4
  • 41
    • 0000211193 scopus 로고
    • Developmental regulation of (1-3, 1-4)-β-glucanase gene expression in barley. Tissue specific expression of individual isoenzymes
    • N. Slakeski, and G.B. Fincher Developmental regulation of (1-3, 1-4)-β-glucanase gene expression in barley. Tissue specific expression of individual isoenzymes Plant Physiol. 99 1992 1226 1231
    • (1992) Plant Physiol. , vol.99 , pp. 1226-1231
    • Slakeski, N.1    Fincher, G.B.2
  • 42
    • 0026673299 scopus 로고
    • Evolution and differential expression of the (1,3)-beta-glucan endohydrolase-encoding gene family in barley, Hordeum vulgare
    • P. Xu, J. Wang, and G.B. Fincher Evolution and differential expression of the (1,3)-beta-glucan endohydrolase-encoding gene family in barley, Hordeum vulgare Gene 120 1992 157 165
    • (1992) Gene , vol.120 , pp. 157-165
    • Xu, P.1    Wang, J.2    Fincher, G.B.3
  • 43
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O. Emanuelsson, H. Nielsen, S. Brunak, and G. von Heijne Predicting subcellular localization of proteins based on their N-terminal amino acid sequence J. Mol. Biol. 300 2000 1005 1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4


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