메뉴 건너뛰기




Volumn 378, Issue 2, 2004, Pages 497-507

Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: Identification of seed proteins targeted by barley thioredoxin h isoforms

Author keywords

Barley seed proteome; Cy5 maleimide labelling; Disulphide reduction; Monobromobimane; Target proteins; Thioredoxin h

Indexed keywords

DYES; ENZYME KINETICS; MASS SPECTROMETRY; SEED;

EID: 1642409412     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031634     Document Type: Article
Times cited : (110)

References (47)
  • 5
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb, N., Thomas, D., Verdoucq, L., Monfort, P. and Meyer, Y. (1998) In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 95, 3312-3317
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 6
    • 0024110181 scopus 로고
    • An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach
    • Florencio, F. J., Yee, B. C., Johnson, T. C. and Buchanan, B. B. (1988) An NADP/thioredoxin system in leaves: purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch. Biochem. Biophys. 266, 496-507
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 496-507
    • Florencio, F.J.1    Yee, B.C.2    Johnson, T.C.3    Buchanan, B.B.4
  • 8
    • 0025944354 scopus 로고
    • Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins
    • Kobrehel, K., Yee, B. C. and Buchanan, B. B. (1991) Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins. J. Biol. Chem. 266, 16135-16140
    • (1991) J. Biol. Chem. , vol.266 , pp. 16135-16140
    • Kobrehel, K.1    Yee, B.C.2    Buchanan, B.B.3
  • 9
    • 0027143431 scopus 로고
    • Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein
    • Jiao, J., Yee, B. C., Wong, J. H., Kobrehel, K. and Buchanan, B. B. (1993) Thioredoxin-linked changes in regulatory properties of barley α-amylase/subtilisin inhibitor protein. Plant Physiol. Biochem. 31, 799-804
    • (1993) Plant Physiol. Biochem. , vol.31 , pp. 799-804
    • Jiao, J.1    Yee, B.C.2    Wong, J.H.3    Kobrehel, K.4    Buchanan, B.B.5
  • 11
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx, C., Wong, J. H. and Buchanan, B. B. (2003) Thioredoxin and germinating barley: targets and protein redox changes. Planta 216, 454-460
    • (2003) Planta , vol.216 , pp. 454-460
    • Marx, C.1    Wong, J.H.2    Buchanan, B.B.3
  • 12
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J. H., Balmer, Y., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J. and Buchanan, B. B. (2003) Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 547, 151-156
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 13
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two dimensional difference gel electrophoresis fluorescent dyes
    • Shaw, J., Roelinson, R., Nickson, J., Stone, T., Sweet, A., Williums, K. and Tonge, R. (2003) Evaluation of saturation labelling two dimensional difference gel electrophoresis fluorescent dyes. Proteomics 3, 1181-1195
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Roelinson, R.2    Nickson, J.3    Stone, T.4    Sweet, A.5    Williums, K.6    Tonge, R.7
  • 14
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extract
    • Unlu, M., Morgan, E. and Minden, J. S. (1997) Difference gel electrophoresis: a single gel method for detecting changes in protein extract. Electrophoresis 18, 2071-2077
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, E.2    Minden, J.S.3
  • 15
    • 0033428817 scopus 로고    scopus 로고
    • Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho, M. J., Wong, J. H., Marx, C., Jiang, W., Lemaux, P. G. and Buchanan, B. B. (1999) Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain. Proc. Natl. Acad. Sci. U.S.A. 96, 14641-14646
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14641-14646
    • Cho, M.J.1    Wong, J.H.2    Marx, C.3    Jiang, W.4    Lemaux, P.G.5    Buchanan, B.B.6
  • 16
    • 0037058928 scopus 로고    scopus 로고
    • Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone
    • Wong, J. H., Kim, Y. B., Ren, P. H., Cai, N., Cho, M. J., Hedden, P., Lemaux, P. G. and Buchanan, B. B. (2002) Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone. Proc. Natl. Acad. Sci. U.S.A. 99, 16325-16330
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16325-16330
    • Wong, J.H.1    Kim, Y.B.2    Ren, P.H.3    Cai, N.4    Cho, M.J.5    Hedden, P.6    Lemaux, P.G.7    Buchanan, B.B.8
  • 17
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from barley seed proteome
    • Maeda, K., Finnie, C., Østergaard, O. and Svensson, B. (2003) Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from barley seed proteome. Eur. J. Biochem. 270, 2633-2643
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Østergaard, O.3    Svensson, B.4
  • 18
  • 19
    • 1542615443 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry
    • DOI 10.1002/pmic.200300615
    • Bak-Jensen, K. S., Laugesen, S., Roepstorff, P. and Svensson, B. (2003) Two-dimensional electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry. Proteomics, DOI 10.1002/pmic.200300615
    • (2003) Proteomics
    • Bak-Jensen, K.S.1    Laugesen, S.2    Roepstorff, P.3    Svensson, B.4
  • 20
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADP thioredoxin reductase cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot, J. P., Rivera-Madrid, R., Marinho, P., Kollarova, M., Maréchal, P. L., Miginiac-Maslow, M. and Meyer, Y. (1994) Arabidopsis thaliana NADP thioredoxin reductase cDNA characterization and expression of the recombinant protein in Escherichia coli. J. Mol. Biol. 235, 1357-1363
    • (1994) J. Mol. Biol. , vol.235 , pp. 1357-1363
    • Jacquot, J.P.1    Rivera-Madrid, R.2    Marinho, P.3    Kollarova, M.4    Maréchal, P.L.5    Miginiac-Maslow, M.6    Meyer, Y.7
  • 21
    • 0032032912 scopus 로고    scopus 로고
    • Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli
    • Gautier, M. F., Lullien-Pellerin, V., de Lamotte-Guery, F., Guirao, A. and Joudrier, P. (1998) Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli. Eur. J. Biochem. 252, 314-324
    • (1998) Eur. J. Biochem. , vol.252 , pp. 314-324
    • Gautier, M.F.1    Lullien-Pellerin, V.2    De Lamotte-Guery, F.3    Guirao, A.4    Joudrier, P.5
  • 22
    • 0035983965 scopus 로고    scopus 로고
    • Proteome analysis of grain filling and seed maturation in barley
    • Finnie, C., Melchior, S., Roepstorff, P. and Svensson, B. (2002) Proteome analysis of grain filling and seed maturation in barley. Plant Physiol. 129, 1308-1319
    • (2002) Plant Physiol. , vol.129 , pp. 1308-1319
    • Finnie, C.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 23
    • 0002426675 scopus 로고    scopus 로고
    • Detection of proteins on two-dimensional electrophoresis gels two-dimensional gel electrophoresis and identification methods
    • Rabilloud, T., ed., Springer-Verlag, Berlin
    • Rabilloud, T. and Charmont, S. (2000) Detection of proteins on two-dimensional electrophoresis gels two-dimensional gel electrophoresis and identification methods. In Proteome Research (Rabilloud, T., ed.), pp. 109-110, Springer-Verlag, Berlin
    • (2000) Proteome Research , pp. 109-110
    • Rabilloud, T.1    Charmont, S.2
  • 24
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 25
    • 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
    • Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R. and Roepstorff, P. (1999) 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, 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
  • 26
    • 0031893286 scopus 로고    scopus 로고
    • Structure of barley grain peroxidase refined at 1.9 Å resolution. A plant peroxidase reversibly inactivated at neutral pH
    • Henriksen, A., Welinder, K. G. and Gajhede, M. (1998) Structure of barley grain peroxidase refined at 1.9 Å resolution. A plant peroxidase reversibly inactivated at neutral pH. J. Biol. Chem. 273, 2241-2248
    • (1998) J. Biol. Chem. , vol.273 , pp. 2241-2248
    • Henriksen, A.1    Welinder, K.G.2    Gajhede, M.3
  • 27
    • 0013505130 scopus 로고
    • Chemical nature of the catalytic sites in glyceraldehyde-3-phosphate dehydrogenase
    • Harris, I., Meriwether, B. P. and Park, J. H. (1963) Chemical nature of the catalytic sites in glyceraldehyde-3-phosphate dehydrogenase. Nature (London) 198, 154-157
    • (1963) Nature (London) , vol.198 , pp. 154-157
    • Harris, I.1    Meriwether, B.P.2    Park, J.H.3
  • 28
    • 0029055108 scopus 로고
    • Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy
    • Strobl, S., Muhlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockshuber, R. and Holak, T. A. (1995) Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy. Biochemistry 34, 8281-8293
    • (1995) Biochemistry , vol.34 , pp. 8281-8293
    • Strobl, S.1    Muhlhahn, P.2    Bernstein, R.3    Wiltscheck, R.4    Maskos, K.5    Wunderlich, M.6    Huber, R.7    Glockshuber, R.8    Holak, T.A.9
  • 30
    • 0032524130 scopus 로고    scopus 로고
    • Barley α-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 Å resolution
    • Vallée, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K. W., Sversson, B. and Haser, R. (1998) Barley α-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 Å resolution. Structure 6, 649-659
    • (1998) Structure , vol.6 , pp. 649-659
    • Vallée, F.1    Kadziola, A.2    Bourne, Y.3    Juy, M.4    Rodenburg, K.W.5    Sversson, B.6    Haser, R.7
  • 31
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T. and Neuhaus, J. M. (1993) The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol. 103, 221-226
    • (1993) Plant Physiol. , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.M.3
  • 32
    • 0026021006 scopus 로고
    • Mutation of a negatively charged amino acid in thioredoxin modifies its reactivety with chloroplastic enzymes
    • de Lamotte-Guery, F., Miginiac-Maslow, M., Decottignies, P., Stein, M., Minard, P. and Jacquot, J. P. (1991) Mutation of a negatively charged amino acid in thioredoxin modifies its reactivety with chloroplastic enzymes. Eur. J. Biochem. 196, 287-294
    • (1991) Eur. J. Biochem. , vol.196 , pp. 287-294
    • Lamotte-Guery, F.1    Miginiac-Maslow, M.2    Decottignies, P.3    Stein, M.4    Minard, P.5    Jacquot, J.P.6
  • 33
    • 0029743311 scopus 로고    scopus 로고
    • Identification of residues of spinach thioredoxin f that influence interactions with target enzymes
    • Geck, M. K., Larimer, F. K. and Hartman, F. C. (1996) Identification of residues of spinach thioredoxin f that influence interactions with target enzymes. J. Biol. Chem. 271, 24736-24740
    • (1996) J. Biol. Chem. , vol.271 , pp. 24736-24740
    • Geck, M.K.1    Larimer, F.K.2    Hartman, F.C.3
  • 34
    • 0032568925 scopus 로고    scopus 로고
    • Role of electrostatic interactions on the affinity of thioredoxin for target proteins. Recognition of chloroplast fructose-1,6-bisphosphatase by mutant Escherichia coli thioredoxins
    • Mora-Garcia, S., Rodriguez-Suarez, R. and Wolosiuk, R. A. (1997) Role of electrostatic interactions on the affinity of thioredoxin for target proteins. Recognition of chloroplast fructose-1,6-bisphosphatase by mutant Escherichia coli thioredoxins. J. Biol. Chem. 273, 16273-16280
    • (1997) J. Biol. Chem. , vol.273 , pp. 16273-16280
    • Mora-Garcia, S.1    Rodriguez-Suarez, R.2    Wolosiuk, R.A.3
  • 35
    • 0002294076 scopus 로고
    • Barley α-amylase/subtilisin inhibitor. Isolation and characterisation
    • Mundy, J., Svendsen, I. and Hejgaard, J. (1983) Barley α-amylase/subtilisin inhibitor. Isolation and characterisation. Carlsberg Res. Commun. 48, 81-91
    • (1983) Carlsberg Res. Commun. , vol.48 , pp. 81-91
    • Mundy, J.1    Svendsen, I.2    Hejgaard, J.3
  • 36
    • 0001432052 scopus 로고
    • An endogenous α-amylase inhibitor in barley kernels
    • Weselake, R. J., MacGregor, A. W. and Hill, R. D. (1983) An endogenous α-amylase inhibitor in barley kernels. Plant Physiol. 72, 809-812
    • (1983) Plant Physiol. , vol.72 , pp. 809-812
    • Weselake, R.J.1    MacGregor, A.W.2    Hill, R.D.3
  • 37
    • 0042835775 scopus 로고    scopus 로고
    • Trypsin/α-amylase inhibitors inactivate the endogenous barley/malt serine endoproteinase SEP-1
    • Jones, B. L. and Fontanini, D. (2003) Trypsin/α-amylase inhibitors inactivate the endogenous barley/malt serine endoproteinase SEP-1. J. Agric. Food Chem. 51, 5803-5814
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 5803-5814
    • Jones, B.L.1    Fontanini, D.2
  • 39
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schulumbaum, A., Mauch, F., Vögeli, U. and Boller, T. (1986) Plant chitinases are potent inhibitors of fungal growth. Nature (London) 324, 365-367
    • (1986) Nature (London) , vol.324 , pp. 365-367
    • Schulumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 40
    • 0027507001 scopus 로고
    • Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina, A., Segura, A. and Garcia-Olmedo, F. (1993) Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett. 316, 119-122
    • (1993) FEBS Lett. , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 41
    • 0030200167 scopus 로고    scopus 로고
    • Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action
    • Yamagami, T. and Funatsu, G. (1996) Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: role of the chitin-binding domain in its chitinase action. Biosci. Biotech. Biochem. 60, 1081-1086
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 1081-1086
    • Yamagami, T.1    Funatsu, G.2
  • 43
    • 0041856169 scopus 로고    scopus 로고
    • Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modification of the peptidyl-prolyl cis-trans isomerase activity
    • Motohashi, K., Koyama, F., Nakanishi, Y. and Ueoka-Nakanishi, H. (2003) Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modification of the peptidyl-prolyl cis-trans isomerase activity. J. Biol. Chem. 278, 31848-31852
    • (2003) J. Biol. Chem. , vol.278 , pp. 31848-31852
    • Motohashi, K.1    Koyama, F.2    Nakanishi, Y.3    Ueoka-Nakanishi, H.4
  • 44
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light-dependent regulation of activity by thiol oxidation and reduction
    • Carr, P. D., Verger, D., Ashton, A. R. and Ollis, D. L. (1999) Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Structure 7, 461-475
    • (1999) Structure , vol.7 , pp. 461-475
    • Carr, P.D.1    Verger, D.2    Ashton, A.R.3    Ollis, D.L.4
  • 47
    • 0028363956 scopus 로고
    • Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana
    • Lippuner, V., Chou, I. T., Scott, S. V., Ettinger, W. F., Theg, S. M. and Gasser, C. S. (1994) Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana. J. Biol. Chem. 269, 7863-7868
    • (1994) J. Biol. Chem. , vol.269 , pp. 7863-7868
    • Lippuner, V.1    Chou, I.T.2    Scott, S.V.3    Ettinger, W.F.4    Theg, S.M.5    Gasser, C.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.