메뉴 건너뛰기




Volumn 177, Issue 6, 2009, Pages 584-592

Engineering increases in sulfur amino acid contents in flax by overexpressing the yeast Met25 gene

Author keywords

Cysteine; Flax; Fusarium; Glutahione; Met25; Transgenic plants

Indexed keywords

FUSARIUM; LINUM USITATISSIMUM;

EID: 70349975989     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2009.08.008     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants
    • Droux M., Ruffet M., Douce R., and Job D. Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. FEBS 255 (1998) 235-245
    • (1998) FEBS , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.2    Douce, R.3    Job, D.4
  • 3
    • 0035989861 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of the enzymes of cysteine biosynthesis in the plant Arabidopsis thaliana
    • Hell R., Jost R., Berkowitz O., and Wirtz M. Molecular and biochemical analysis of the enzymes of cysteine biosynthesis in the plant Arabidopsis thaliana. Amino Acids 22 (2002) 245-257
    • (2002) Amino Acids , vol.22 , pp. 245-257
    • Hell, R.1    Jost, R.2    Berkowitz, O.3    Wirtz, M.4
  • 4
    • 0034078554 scopus 로고    scopus 로고
    • Regulation of sulfate transport and synthesis of sulfur-containing amino acids
    • Saito K. Regulation of sulfate transport and synthesis of sulfur-containing amino acids. Curr. Opin. Plant Biol. 3 (2000) 188-195
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 188-195
    • Saito, K.1
  • 5
    • 0033213374 scopus 로고    scopus 로고
    • Increased resistance to oxidative stress in transgenic tobacco plants overexpressing bacterial serine acetyltransferase
    • Blaszczyk A., Brodzik R., and Sirko A. Increased resistance to oxidative stress in transgenic tobacco plants overexpressing bacterial serine acetyltransferase. Plant J. 20 (1999) 237-243
    • (1999) Plant J. , vol.20 , pp. 237-243
    • Blaszczyk, A.1    Brodzik, R.2    Sirko, A.3
  • 6
    • 0034088162 scopus 로고    scopus 로고
    • Expression of a bacterial serine acetyltransferase in transgenic potato plants leads to increased levels of cysteine and glutathione
    • Harms K., Ballmoo P.V., Brunold C., Höfgen R., and Hesse H. Expression of a bacterial serine acetyltransferase in transgenic potato plants leads to increased levels of cysteine and glutathione. Plant J. 22 (2000) 335-343
    • (2000) Plant J. , vol.22 , pp. 335-343
    • Harms, K.1    Ballmoo, P.V.2    Brunold, C.3    Höfgen, R.4    Hesse, H.5
  • 7
    • 0037354077 scopus 로고    scopus 로고
    • Production of cysteine for bacterial and plant biotechnology: application of cysteine feedback-insensitive isoforms of serine acetyltransferase
    • Wirtz M., and Hell R. Production of cysteine for bacterial and plant biotechnology: application of cysteine feedback-insensitive isoforms of serine acetyltransferase. Amino Acids 24 (2003) 195-203
    • (2003) Amino Acids , vol.24 , pp. 195-203
    • Wirtz, M.1    Hell, R.2
  • 8
    • 33645236871 scopus 로고    scopus 로고
    • Transgenic tobacco plants overexpressing the Met25 gene of Saccharomyces cerevisiae exhibit enhanced levels of cysteine and glutathione and increased tolerance to oxidative stress
    • Matityahu I., Kachan L., Bar Ilan I., and Amir R. Transgenic tobacco plants overexpressing the Met25 gene of Saccharomyces cerevisiae exhibit enhanced levels of cysteine and glutathione and increased tolerance to oxidative stress. Amino Acids 30 (2006) 185-194
    • (2006) Amino Acids , vol.30 , pp. 185-194
    • Matityahu, I.1    Kachan, L.2    Bar Ilan, I.3    Amir, R.4
  • 9
    • 4344651169 scopus 로고    scopus 로고
    • Overproduction of SAT and/or OASTL in transgenic plants: a survey of effects
    • Sirko A., Blaszczyk A., and Liszewska F. Overproduction of SAT and/or OASTL in transgenic plants: a survey of effects. J. Exp. Bot. 55 (2004) 1881-1888
    • (2004) J. Exp. Bot. , vol.55 , pp. 1881-1888
    • Sirko, A.1    Blaszczyk, A.2    Liszewska, F.3
  • 10
    • 4344654883 scopus 로고    scopus 로고
    • Analysis of transgenic tobacco lines expressing bacterial cysK gene encoding O-acetylserine (thiol) lyase A
    • Davidian J.-C., Grill D., De Kok L.J., Stulen I., Hawkesford M.J., Schnug E., and Rennerberg H. (Eds), Backhuys Publishers, Leiden
    • Liszewska F., and Sirko A. Analysis of transgenic tobacco lines expressing bacterial cysK gene encoding O-acetylserine (thiol) lyase A. In: Davidian J.-C., Grill D., De Kok L.J., Stulen I., Hawkesford M.J., Schnug E., and Rennerberg H. (Eds). Sulphur Transport and Assimilation in Plants. Regulation, Interaction and Signaling (2003), Backhuys Publishers, Leiden 269-271
    • (2003) Sulphur Transport and Assimilation in Plants. Regulation, Interaction and Signaling , pp. 269-271
    • Liszewska, F.1    Sirko, A.2
  • 11
    • 0347236863 scopus 로고    scopus 로고
    • Modification of non-protein thiols contents in transgenic tobacco plants producing bacterial enzymes of cysteine biosynthesis pathway
    • Liszewska F., Blaszczyk A., and Sirko A. Modification of non-protein thiols contents in transgenic tobacco plants producing bacterial enzymes of cysteine biosynthesis pathway. Acta Biochim. Pol. 48 (2001) 647-656
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 647-656
    • Liszewska, F.1    Blaszczyk, A.2    Sirko, A.3
  • 12
    • 0034953859 scopus 로고    scopus 로고
    • Cysteine synthase overexpression in tobacco confers tolerance to sulfur-containing environmental pollutant
    • Noji M., Saito M., Nakamura M., Aono M., Saji H., and Saito K. Cysteine synthase overexpression in tobacco confers tolerance to sulfur-containing environmental pollutant. Plant Physiol. 126 (2001) 973-980
    • (2001) Plant Physiol. , vol.126 , pp. 973-980
    • Noji, M.1    Saito, M.2    Nakamura, M.3    Aono, M.4    Saji, H.5    Saito, K.6
  • 13
    • 0028534746 scopus 로고
    • Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase [O-acetylserine(thiol)-lyase]
    • Saito K., Kurosawa M., Tatsuguchi K., Takagi Y., and Murakoshi I. Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase [O-acetylserine(thiol)-lyase]. Plant Physiol. 106 (1994) 887-895
    • (1994) Plant Physiol. , vol.106 , pp. 887-895
    • Saito, K.1    Kurosawa, M.2    Tatsuguchi, K.3    Takagi, Y.4    Murakoshi, I.5
  • 14
    • 0034948328 scopus 로고    scopus 로고
    • Increased cysteine biosynthesis capacity of transgenic tobacco overexpressing an O-acetylserine(thiol) lyase modifies plant responses to oxidative stress
    • Youssefian S., Nakamura M., Orudgev E., and Kondo N. Increased cysteine biosynthesis capacity of transgenic tobacco overexpressing an O-acetylserine(thiol) lyase modifies plant responses to oxidative stress. Plant Physiol. 126 (2001) 1001-1011
    • (2001) Plant Physiol. , vol.126 , pp. 1001-1011
    • Youssefian, S.1    Nakamura, M.2    Orudgev, E.3    Kondo, N.4
  • 15
    • 0027688450 scopus 로고
    • Tobacco plants transformed with the O-acetylserine (thiol) lyase gene of wheat are resistant to toxic levels of hydrogen sulphide gas
    • Youssefian S., Nakamura M., and Sano H. Tobacco plants transformed with the O-acetylserine (thiol) lyase gene of wheat are resistant to toxic levels of hydrogen sulphide gas. Plant J. 4 (1993) 759-769
    • (1993) Plant J. , vol.4 , pp. 759-769
    • Youssefian, S.1    Nakamura, M.2    Sano, H.3
  • 16
    • 0027320121 scopus 로고
    • Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment
    • Cherest H., Thomas D., and Surdin-Kerjan Y. Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment. J. Bacteriol. 175 (1993) 5366-5374
    • (1993) J. Bacteriol. , vol.175 , pp. 5366-5374
    • Cherest, H.1    Thomas, D.2    Surdin-Kerjan, Y.3
  • 17
    • 0041834714 scopus 로고    scopus 로고
    • In vivo analysis of various substrates utilized by cystathionine {gamma}-synthase and o-acetylhomoserine sulfhydrylase in methionine biosynthesis
    • Hacham Y., Gophna U., and Amir R. In vivo analysis of various substrates utilized by cystathionine {gamma}-synthase and o-acetylhomoserine sulfhydrylase in methionine biosynthesis. Mol. Biol. Evol. 20 (2003) 1513-1520
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 1513-1520
    • Hacham, Y.1    Gophna, U.2    Amir, R.3
  • 18
    • 0016499866 scopus 로고
    • O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast; studies with methionine auxotrophs
    • Yamagata S., Takeshima K., and Naiki N. O-acetylserine and O-acetylhomoserine sulfhydrylase of yeast; studies with methionine auxotrophs. J. Biochem. 77 (1975) 1029-1036
    • (1975) J. Biochem. , vol.77 , pp. 1029-1036
    • Yamagata, S.1    Takeshima, K.2    Naiki, N.3
  • 19
    • 0028171941 scopus 로고
    • Overexpression of the saccharomyces cerevisiae MET17/MET25 gene in Escherichia coli and comparative characterization of the product with O-acetylserine. O-acetylhomoserine sulhydrylase of the yeast
    • Yamagata S., Isaji M., Nakamura K., Fujisaki S., Doi K., Bawden S., et al. Overexpression of the saccharomyces cerevisiae MET17/MET25 gene in Escherichia coli and comparative characterization of the product with O-acetylserine. O-acetylhomoserine sulhydrylase of the yeast. Appl. Microbiol. Biotechnol. 42 (1994) 92-99
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 92-99
    • Yamagata, S.1    Isaji, M.2    Nakamura, K.3    Fujisaki, S.4    Doi, K.5    Bawden, S.6
  • 20
    • 20444465757 scopus 로고    scopus 로고
    • Impact of reduced O-acetylserine(thiol)lyase isoform contents on potato plant metabolism
    • Riemenschneider A., Riede K., Hoefgen R., Papenbrock J., and Hesse H. Impact of reduced O-acetylserine(thiol)lyase isoform contents on potato plant metabolism. Plant Physiol. 137 (2005) 892-900
    • (2005) Plant Physiol. , vol.137 , pp. 892-900
    • Riemenschneider, A.1    Riede, K.2    Hoefgen, R.3    Papenbrock, J.4    Hesse, H.5
  • 21
    • 0001514394 scopus 로고
    • Glutathione metabolism in plants
    • De Kok L.J. (Ed), SPB Academic Publishing, The Hague, The Netherlands
    • Bergmann L., and Rennenberg H. Glutathione metabolism in plants. In: De Kok L.J. (Ed). Sulfur Nutrition and Assimilation in Higher Plants (1993), SPB Academic Publishing, The Hague, The Netherlands 109-123
    • (1993) Sulfur Nutrition and Assimilation in Higher Plants , pp. 109-123
    • Bergmann, L.1    Rennenberg, H.2
  • 22
    • 0034979751 scopus 로고    scopus 로고
    • The biological functions of glutathione revisited in arabidopsis transgenic plants with altered glutathione levels
    • Xiang C., Werner B.L., Christensen E.M., and Oliver D.J. The biological functions of glutathione revisited in arabidopsis transgenic plants with altered glutathione levels. Plant Physiol. 126 (2001) 564-574
    • (2001) Plant Physiol. , vol.126 , pp. 564-574
    • Xiang, C.1    Werner, B.L.2    Christensen, E.M.3    Oliver, D.J.4
  • 23
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione s-transferases in plants
    • Marrs K.A. The functions and regulation of glutathione s-transferases in plants. Annu. Rev. Plant. Physiol. Plant Mol. Biol. 47 (1996) 127-158
    • (1996) Annu. Rev. Plant. Physiol. Plant Mol. Biol. , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 24
    • 0036001080 scopus 로고    scopus 로고
    • Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signalling
    • Noctor G., Gomez L., Vanacker H., and Foyer C.H. Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signalling. J. Exp. Bot. 53 (2002) 1283-1304
    • (2002) J. Exp. Bot. , vol.53 , pp. 1283-1304
    • Noctor, G.1    Gomez, L.2    Vanacker, H.3    Foyer, C.H.4
  • 25
    • 0036619361 scopus 로고    scopus 로고
    • Differential effects of H2S on cytoplasmic and nuclear thiol concentrations in different tissues of Brassica roots
    • Müller M., De Kok L.J., Weidner W., and Tausz M. Differential effects of H2S on cytoplasmic and nuclear thiol concentrations in different tissues of Brassica roots. Plant Physiol. Biochem. 40 (2002) 585-589
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 585-589
    • Müller, M.1    De Kok, L.J.2    Weidner, W.3    Tausz, M.4
  • 26
    • 0029137960 scopus 로고
    • et al, Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing glutathione synthetase
    • Strohm M., Jouanin L., Kunert K.J., Pruvost C., Polle A., and Foyer C.H. et al, Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing glutathione synthetase. Plant J. 7 (1995) 141-145
    • (1995) Plant J. , vol.7 , pp. 141-145
    • Strohm, M.1    Jouanin, L.2    Kunert, K.J.3    Pruvost, C.4    Polle, A.5    Foyer, C.H.6
  • 27
    • 0029749087 scopus 로고    scopus 로고
    • Synthesis of glutathione in leaves of transgenic poplar overexpressing [gamma]-glutamylcysteine synthetase
    • Noctor G., Strohm M., Jouanin L., Kunert K.J., Foyer C.H., and Rennenberg H. Synthesis of glutathione in leaves of transgenic poplar overexpressing [gamma]-glutamylcysteine synthetase. Plant Physiol. 112 (1996) 1071-1078
    • (1996) Plant Physiol. , vol.112 , pp. 1071-1078
    • Noctor, G.1    Strohm, M.2    Jouanin, L.3    Kunert, K.J.4    Foyer, C.H.5    Rennenberg, H.6
  • 28
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobaccotissue culture
    • Murashige T., and Skoog F. A revised medium for rapid growth and bioassays with tobaccotissue culture. Physiol. Plantarum (1962) 473-497
    • (1962) Physiol. Plantarum , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 30
    • 0037402742 scopus 로고    scopus 로고
    • Rocket-powered high-performance liquid chromatographic analysis of plant ascorbate and glutathione
    • Davey M.W., Dekempeneer E., and Keulemans J. Rocket-powered high-performance liquid chromatographic analysis of plant ascorbate and glutathione. Anal. Biochem. 316 (2003) 74-81
    • (2003) Anal. Biochem. , vol.316 , pp. 74-81
    • Davey, M.W.1    Dekempeneer, E.2    Keulemans, J.3
  • 31
    • 33748975884 scopus 로고    scopus 로고
    • Development of a fluorescence-based microtiter plate method for the measurement of glutathione in yeast
    • Lewicki K., Marchand S., Matoub L., Lulek J., Coulon J., and Leroy P. Development of a fluorescence-based microtiter plate method for the measurement of glutathione in yeast. Talanta 70 (2006) 876-882
    • (2006) Talanta , vol.70 , pp. 876-882
    • Lewicki, K.1    Marchand, S.2    Matoub, L.3    Lulek, J.4    Coulon, J.5    Leroy, P.6
  • 32
    • 27644463015 scopus 로고    scopus 로고
    • Assessment of in situ cellular glutathione labeling with naphthalene-2, 3-dicarboxaldehyde using high-performance liquid chromatography
    • Diez L., Martenka E., Dabrowska A., Coulon J., and Leroy P. Assessment of in situ cellular glutathione labeling with naphthalene-2, 3-dicarboxaldehyde using high-performance liquid chromatography. J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 827 (2005) 44-50
    • (2005) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.827 , pp. 44-50
    • Diez, L.1    Martenka, E.2    Dabrowska, A.3    Coulon, J.4    Leroy, P.5
  • 33
    • 85072188824 scopus 로고
    • Thiobarbituric acid assay reactants
    • Aust S.D. Thiobarbituric acid assay reactants. Methods Toxicol. 1B (1994) 367-374
    • (1994) Methods Toxicol. , vol.1 B , pp. 367-374
    • Aust, S.D.1
  • 34
    • 0023161313 scopus 로고
    • Molecular genetics of met 17 and met 25 mutants of Saccharomyces cerevisiae: intragenic complementation between mutations of a single structural gene
    • D'Andrea R., Surdin-Kerjan Y., Pure G., and Cherest H. Molecular genetics of met 17 and met 25 mutants of Saccharomyces cerevisiae: intragenic complementation between mutations of a single structural gene. Mol. Gen. Genet. 207 (1987) 165-170
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 165-170
    • D'Andrea, R.1    Surdin-Kerjan, Y.2    Pure, G.3    Cherest, H.4
  • 35
    • 0031457095 scopus 로고    scopus 로고
    • Metabolism of sulfur amino acids in Saccharomyces cerevisiae
    • Thomas D., and Surdin-Kerjan Y. Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 61 (1997) 503-532
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 503-532
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 36
    • 33750315393 scopus 로고    scopus 로고
    • Methionine catabolism in Arabidopsis cells is initiated by a γ-cleavage process and leads to S-methylcysteine and isoleucine syntheses
    • Rebeille F., Jabrin S., Bligny R., Loizeau K., Gambonnet B., Van Wilder V., et al. Methionine catabolism in Arabidopsis cells is initiated by a γ-cleavage process and leads to S-methylcysteine and isoleucine syntheses. PNAS 103 (2006) 15687-15692
    • (2006) PNAS , vol.103 , pp. 15687-15692
    • Rebeille, F.1    Jabrin, S.2    Bligny, R.3    Loizeau, K.4    Gambonnet, B.5    Van Wilder, V.6
  • 37
    • 0000173522 scopus 로고
    • Primary and secondary metabolism of polyamines in plants
    • Poulton J.E., Romeo J.T., and Conn E.E. (Eds), Plenum Press, New York (Rec. Adv. Phytochem.)
    • Flores H., Protacio C., and Signs M. Primary and secondary metabolism of polyamines in plants. In: Poulton J.E., Romeo J.T., and Conn E.E. (Eds). Plant Nitrogen Metabolism (1989), Plenum Press, New York 329-393 (Rec. Adv. Phytochem.)
    • (1989) Plant Nitrogen Metabolism , pp. 329-393
    • Flores, H.1    Protacio, C.2    Signs, M.3
  • 38
    • 20144374948 scopus 로고
    • The formation of amines and their derivatives in plants
    • Hewitt E.J., and Cutting C.V. (Eds), Academic Press, New York
    • Smith T., and Bagni N. The formation of amines and their derivatives in plants. In: Hewitt E.J., and Cutting C.V. (Eds). Nitrogen Assimilation of Plants (1979), Academic Press, New York 557-570
    • (1979) Nitrogen Assimilation of Plants , pp. 557-570
    • Smith, T.1    Bagni, N.2
  • 40
    • 0001575175 scopus 로고
    • Purification and characterization of cysteine synthase from Citrullus vulgaris
    • Ikegami F., Kaneko M., Kaneko H., and Murakoshi I. Purification and characterization of cysteine synthase from Citrullus vulgaris. Phytochemistry (1988) 697-701
    • (1988) Phytochemistry , pp. 697-701
    • Ikegami, F.1    Kaneko, M.2    Kaneko, H.3    Murakoshi, I.4
  • 41
    • 4344606519 scopus 로고    scopus 로고
    • Elemental sulphur as an induced antifungal substance in plant defence
    • Cooper R.M., and Williams J.S. Elemental sulphur as an induced antifungal substance in plant defence. J. Exp. Bot. 55 (2004) 1947-1953
    • (2004) J. Exp. Bot. , vol.55 , pp. 1947-1953
    • Cooper, R.M.1    Williams, J.S.2
  • 42
    • 25844477540 scopus 로고    scopus 로고
    • Sulfur metabolism: a versatile platform for launching defence operations
    • Rausch T., and Wachter A. Sulfur metabolism: a versatile platform for launching defence operations. Trends Plants Sci. 10 (2005) 503-509
    • (2005) Trends Plants Sci. , vol.10 , pp. 503-509
    • Rausch, T.1    Wachter, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.