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Volumn 20, Issue 1, 2008, Pages 168-185

Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 43549120312     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.107.056747     Document Type: Article
Times cited : (202)

References (74)
  • 1
    • 0000128999 scopus 로고
    • Sulfide inhibition in rice roots
    • Allam, A.I., and Hollis, J.P. (1972). Sulfide inhibition in rice roots. Phytopathology 62: 634-639.
    • (1972) Phytopathology , vol.62 , pp. 634-639
    • Allam, A.I.1    Hollis, J.P.2
  • 2
    • 0037163108 scopus 로고    scopus 로고
    • Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from Arabidopsis thaliana
    • Berkowitz, O., Wirtz, M., Wolf, A., Kuhlmann, J., and Hell, R. (2002). Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from Arabidopsis thaliana. J. Biol. Chem. 277: 30629-30634.
    • (2002) J. Biol. Chem , vol.277 , pp. 30629-30634
    • Berkowitz, O.1    Wirtz, M.2    Wolf, A.3    Kuhlmann, J.4    Hell, R.5
  • 3
    • 0028938619 scopus 로고
    • Cysteine biosynthesis in plants: Isolation and functional identification of a cDNA encoding a serine acetyltransferase from Arabidopsis thaliana
    • Bogdanova, N., Bork, C., and Hell, R. (1995). Cysteine biosynthesis in plants: Isolation and functional identification of a cDNA encoding a serine acetyltransferase from Arabidopsis thaliana. FEBS Lett. 358: 43-47.
    • (1995) FEBS Lett , vol.358 , pp. 43-47
    • Bogdanova, N.1    Bork, C.2    Hell, R.3
  • 4
    • 0031079570 scopus 로고    scopus 로고
    • Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana
    • Bogdanova, N., and Hell, R. (1997). Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana. Plant J. 11: 251-262.
    • (1997) Plant J , vol.11 , pp. 251-262
    • Bogdanova, N.1    Hell, R.2
  • 5
    • 33644685874 scopus 로고    scopus 로고
    • Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
    • Bonner, E.R., Cahoon, R.E., Knapke, S.M., and Jez, J.M. (2005). Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana. J. Biol. Chem. 280: 38803-38813.
    • (2005) J. Biol. Chem , vol.280 , pp. 38803-38813
    • Bonner, E.R.1    Cahoon, R.E.2    Knapke, S.M.3    Jez, J.M.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0000485535 scopus 로고
    • Intracellular localization of serine acetyltransferase in spinach leaves
    • Brunold, C., and Suter, M. (1982). Intracellular localization of serine acetyltransferase in spinach leaves. Planta 155: 321-327.
    • (1982) Planta , vol.155 , pp. 321-327
    • Brunold, C.1    Suter, M.2
  • 8
    • 0033103063 scopus 로고    scopus 로고
    • Generation of enhancer trap lines in Arabidopsis and characterization of expression patterns in the inflorescence
    • Campisi, L., Yang, Y., Yi, Y., Heilig, E., Herman, B., Cassista, A.J., Allen, D.W., Xiang, H., and Jack, T. (1999). Generation of enhancer trap lines in Arabidopsis and characterization of expression patterns in the inflorescence. Plant J. 17: 699-707.
    • (1999) Plant J , vol.17 , pp. 699-707
    • Campisi, L.1    Yang, Y.2    Yi, Y.3    Heilig, E.4    Herman, B.5    Cassista, A.J.6    Allen, D.W.7    Xiang, H.8    Jack, T.9
  • 9
    • 33745060757 scopus 로고    scopus 로고
    • Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei
    • Colasante, C., Ellis, M., Ruppert, T., and Voncken, F. (2006). Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics 6: 3275-3293.
    • (2006) Proteomics , vol.6 , pp. 3275-3293
    • Colasante, C.1    Ellis, M.2    Ruppert, T.3    Voncken, F.4
  • 11
    • 51249186914 scopus 로고    scopus 로고
    • Dellaporta, S.L., Wood, J., Hicks, J. B. (1982). A plant DNA minipreparation: Version II. Plant Mol. Biol. Rep. 1: 19-21.
    • Dellaporta, S.L., Wood, J., Hicks, J. B. (1982). A plant DNA minipreparation: Version II. Plant Mol. Biol. Rep. 1: 19-21.
  • 12
    • 0242584820 scopus 로고    scopus 로고
    • Plant serine acetyltransferase: New insights for regulation of sulphur metabolism in plant cells
    • Droux, M. (2003). Plant serine acetyltransferase: New insights for regulation of sulphur metabolism in plant cells. Plant Physiol. Biochem. 41: 619-627.
    • (2003) Plant Physiol. Biochem , vol.41 , pp. 619-627
    • Droux, M.1
  • 13
    • 1642308088 scopus 로고    scopus 로고
    • Sulfur assimilation and the role of sulfur in plant metabolism: A survey
    • Droux, M. (2004). Sulfur assimilation and the role of sulfur in plant metabolism: A survey. Photosynth. Res. 79: 331-348.
    • (2004) Photosynth. Res , vol.79 , pp. 331-348
    • Droux, M.1
  • 14
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - Structural and kinetic properties of the free and bound enzymes
    • Droux, M., Ruffet, M.L., Douce, R., and Job, D. (1998). Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - Structural and kinetic properties of the free and bound enzymes. Eur. J. Biochem. 255: 235-245.
    • (1998) Eur. J. Biochem , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.L.2    Douce, R.3    Job, D.4
  • 17
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
    • Francois, J.A., Kumaran, S., and Jez, J.M. (2006). Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex. Plant Cell 18: 3647-3655.
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 18
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occuring amino acids
    • Gaitonde, M.K. (1967). A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occuring amino acids. Biochem. J. 104: 627-633.
    • (1967) Biochem. J , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 19
    • 34250798528 scopus 로고    scopus 로고
    • γ-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
    • Grzam, A., Martin, M., Hell, R., and Meyer, A. (2007). γ-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis. FEBS Lett. 581: 3131-3138.
    • (2007) FEBS Lett , vol.581 , pp. 3131-3138
    • Grzam, A.1    Martin, M.2    Hell, R.3    Meyer, A.4
  • 20
    • 19944429581 scopus 로고    scopus 로고
    • Characterization of a T-DNA insertion mutant for the protein import receptor atToc33 from chloroplasts
    • Gutensohn, M., et al. (2004). Characterization of a T-DNA insertion mutant for the protein import receptor atToc33 from chloroplasts. Mol. Genet. Genomics 272: 379-396.
    • (2004) Mol. Genet. Genomics , vol.272 , pp. 379-396
    • Gutensohn, M.1
  • 21
    • 0033927405 scopus 로고    scopus 로고
    • β-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis
    • Hatzfeld, Y., Maruyama, A., Schmidt, A., Noji, M., Ishizawa, K., and Saito, K. (2000). β-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis. Plant Physiol. 123: 1163-1172.
    • (2000) Plant Physiol , vol.123 , pp. 1163-1172
    • Hatzfeld, Y.1    Maruyama, A.2    Schmidt, A.3    Noji, M.4    Ishizawa, K.5    Saito, K.6
  • 22
    • 0030904866 scopus 로고    scopus 로고
    • Molecular physiology of plant sulfur metabolism
    • Hell, R. (1997). Molecular physiology of plant sulfur metabolism. Planta 202: 138-148.
    • (1997) Planta , vol.202 , pp. 138-148
    • Hell, R.1
  • 23
    • 0028025227 scopus 로고
    • Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
    • Hell, R., Bork, C., Bogdanova, N., Frolov, I., and Hauschild, R. (1994). Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana. FEBS Lett. 351: 257-262.
    • (1994) FEBS Lett , vol.351 , pp. 257-262
    • Hell, R.1    Bork, C.2    Bogdanova, N.3    Frolov, I.4    Hauschild, R.5
  • 24
    • 0035313606 scopus 로고    scopus 로고
    • Plant concepts for mineral acquisition and allocation
    • Hell, R., and Hillebrand, H. (2001). Plant concepts for mineral acquisition and allocation. Curr. Opin. Biotechnol. 12: 161-168.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 161-168
    • Hell, R.1    Hillebrand, H.2
  • 25
    • 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. (2002). Molecular and biochemical analysis of the enzymes of cysteine biosynthesis in the plant Arabidopsis thaliana. Amino Acids 22: 245-257.
    • (2002) Amino Acids , vol.22 , pp. 245-257
    • Hell, R.1    Jost, R.2    Berkowitz, O.3    Wirtz, M.4
  • 26
    • 0032915394 scopus 로고    scopus 로고
    • Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana
    • Hesse, H., Lipke, J., Altmann, T., and Hofgen, R. (1999). Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana. Amino Acids 16: 113-131.
    • (1999) Amino Acids , vol.16 , pp. 113-131
    • Hesse, H.1    Lipke, J.2    Altmann, T.3    Hofgen, R.4
  • 27
    • 0344177200 scopus 로고    scopus 로고
    • Global expression profiling of sulfur-starved Arabidopsis by DNA macroarray reveals the role of O-acetyl-L-serine as a general regulator of gene expression in response to sulfur nutrition
    • Hirai, M., Fujiwara, T., Awazuhara, M., Kimura, T., Noji, M., and Saito, K. (2003). Global expression profiling of sulfur-starved Arabidopsis by DNA macroarray reveals the role of O-acetyl-L-serine as a general regulator of gene expression in response to sulfur nutrition. Plant J. 33: 651-663.
    • (2003) Plant J , vol.33 , pp. 651-663
    • Hirai, M.1    Fujiwara, T.2    Awazuhara, M.3    Kimura, T.4    Noji, M.5    Saito, K.6
  • 28
    • 84966453197 scopus 로고
    • The kinetics of penetration. XII. Hydrogen sulfide
    • Jacques, A.G. (1936). The kinetics of penetration. XII. Hydrogen sulfide. J. Gen. Physiol. 19: 397-418.
    • (1936) J. Gen. Physiol , vol.19 , pp. 397-418
    • Jacques, A.G.1
  • 29
    • 0034622527 scopus 로고    scopus 로고
    • Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana
    • Jost, R., Berkowitz, O., Wirtz, M., Hopkins, L., Hawkesford, M.J., and Hell, R. (2000). Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana. Gene 253: 237-247.
    • (2000) Gene , vol.253 , pp. 237-247
    • Jost, R.1    Berkowitz, O.2    Wirtz, M.3    Hopkins, L.4    Hawkesford, M.J.5    Hell, R.6
  • 30
    • 18744378318 scopus 로고    scopus 로고
    • Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis
    • Kawashima, C.G., Berkowitz, O., Hell, R., Noji, M., and Saito, K. (2005). Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis. Plant Physiol. 137: 220-230.
    • (2005) Plant Physiol , vol.137 , pp. 220-230
    • Kawashima, C.G.1    Berkowitz, O.2    Hell, R.3    Noji, M.4    Saito, K.5
  • 31
    • 33645067392 scopus 로고    scopus 로고
    • Regulation of sulfate assimilation in Arabidopsis and beyond
    • Kopriva, S. (2006). Regulation of sulfate assimilation in Arabidopsis and beyond. Ann. Bot. (Lond.) 97: 479-495.
    • (2006) Ann. Bot. (Lond.) , vol.97 , pp. 479-495
    • Kopriva, S.1
  • 32
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • Kredich, N.M., Becker, M.A., and Tomkins, G.M. (1969). Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J. Biol. Chem. 244: 2428-2439.
    • (1969) J. Biol. Chem , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 33
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jansch, L., Werhahn, W., and Braun, H.-P. (2001). Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127: 1694-1710.
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.-P.5
  • 34
    • 0030442921 scopus 로고    scopus 로고
    • Subcellular location of O-acetylserine sulfhydrylase isoenzymes in cell cultures and plant tissues of Datura innoxia Mill
    • Kuske, C.R., Hill, K.K., Guzman, E., and Jackson, P.J. (1996). Subcellular location of O-acetylserine sulfhydrylase isoenzymes in cell cultures and plant tissues of Datura innoxia Mill. Plant Physiol. 112: 659-667.
    • (1996) Plant Physiol , vol.112 , pp. 659-667
    • Kuske, C.R.1    Hill, K.K.2    Guzman, E.3    Jackson, P.J.4
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0034486633 scopus 로고    scopus 로고
    • Pathways and regulation of sulfur metabolism revealed through molecular and genetic studies
    • Leustek, T., Martin, M.N., Bick, J.-A., and Davies, J.P. (2000). Pathways and regulation of sulfur metabolism revealed through molecular and genetic studies. Annu. Rev. Plant Physiol. Plant Mol. Biol. 51: 141-165.
    • (2000) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.51 , pp. 141-165
    • Leustek, T.1    Martin, M.N.2    Bick, J.-A.3    Davies, J.P.4
  • 38
    • 0032841269 scopus 로고    scopus 로고
    • Sulfate transport and assimilation in plants
    • Leustek, T., and Saito, K. (1999). Sulfate transport and assimilation in plants. Plant Physiol. 120: 637-644.
    • (1999) Plant Physiol , vol.120 , pp. 637-644
    • Leustek, T.1    Saito, K.2
  • 39
    • 0001113803 scopus 로고
    • Localization of ATP-sulfurylase and O-acetylserine(thiol)lyase in spinach leaves
    • Lunn, J.E., Droux, M., Martin, J., and Douce, R. (1990). Localization of ATP-sulfurylase and O-acetylserine(thiol)lyase in spinach leaves. Plant Physiol. 94: 1345-1352.
    • (1990) Plant Physiol , vol.94 , pp. 1345-1352
    • Lunn, J.E.1    Droux, M.2    Martin, J.3    Douce, R.4
  • 41
    • 34547885780 scopus 로고    scopus 로고
    • Localization of members of the gamma-glutamyl transpeptidase family identifies sites of glutathione and glutathione S-conjugate hydrolysis
    • Martin, M.N., Saladores, P.H., Lambert, E., Hudson, A.O., and Leustek, T. (2007). Localization of members of the gamma-glutamyl transpeptidase family identifies sites of glutathione and glutathione S-conjugate hydrolysis. Plant Physiol. 144: 1715-1732.
    • (2007) Plant Physiol , vol.144 , pp. 1715-1732
    • Martin, M.N.1    Saladores, P.H.2    Lambert, E.3    Hudson, A.O.4    Leustek, T.5
  • 43
    • 0035316451 scopus 로고    scopus 로고
    • Increase in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex
    • Mino, K., Imamura, K., Sakiyama, T., Eisaki, N., Matsuyama, A., and Nakanishi, K. (2001). Increase in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex. Biosci. Biotechnol. Biochem. 65: 865-874.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 865-874
    • Mino, K.1    Imamura, K.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 44
    • 0034782249 scopus 로고    scopus 로고
    • Miranda, M., Borisjuk, L., Tewes, A., Heim, U., Sauer, N., Wobus, U., and Weber, H. (2001). Amino acid permeases in developing seeds of Vicia faba L.: Expression precedes storage protein synthesis and is regulated by amino acid supply. Plant J. 28: 61-71.
    • Miranda, M., Borisjuk, L., Tewes, A., Heim, U., Sauer, N., Wobus, U., and Weber, H. (2001). Amino acid permeases in developing seeds of Vicia faba L.: Expression precedes storage protein synthesis and is regulated by amino acid supply. Plant J. 28: 61-71.
  • 45
    • 0000760333 scopus 로고
    • Measurement of serine acetyltransferase activity in crude plant extracts by a coupled assay system using cysteine synthase
    • Nakamura, K., Hayama, A., Masada, M., Fukushima, K., and Tamura, G. (1987). Measurement of serine acetyltransferase activity in crude plant extracts by a coupled assay system using cysteine synthase. Plant Cell Physiol. 28: 885-891.
    • (1987) Plant Cell Physiol , vol.28 , pp. 885-891
    • Nakamura, K.1    Hayama, A.2    Masada, M.3    Fukushima, K.4    Tamura, G.5
  • 46
    • 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. (2002). Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signalling. J. Exp. Bot. 53: 1283-1304.
    • (2002) J. Exp. Bot , vol.53 , pp. 1283-1304
    • Noctor, G.1    Gomez, L.2    Vanacker, H.3    Foyer, C.H.4
  • 47
    • 0032483994 scopus 로고    scopus 로고
    • Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
    • Noji, M., Inoue, K., Kimura, N., Gouda, A., and Saito, K. (1998). Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana. J. Biol. Chem. 273: 32739-32745.
    • (1998) J. Biol. Chem , vol.273 , pp. 32739-32745
    • Noji, M.1    Inoue, K.2    Kimura, N.3    Gouda, A.4    Saito, K.5
  • 48
    • 33847148080 scopus 로고    scopus 로고
    • Characterization of the extracellular gamma-glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis
    • Ohkama-Ohtsu, N., Radwan, S., Peterson, A., Zhao, P., Badr, A., Xiang, C., and Oliver, D. (2007a). Characterization of the extracellular gamma-glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis. Plant J. 49: 865-877.
    • (2007) Plant J , vol.49 , pp. 865-877
    • Ohkama-Ohtsu, N.1    Radwan, S.2    Peterson, A.3    Zhao, P.4    Badr, A.5    Xiang, C.6    Oliver, D.7
  • 49
    • 33847169054 scopus 로고    scopus 로고
    • Glutathione conjugates in the vacuole are degraded by gamma-glutamyl transpeptidase GGT3 in Arabidopsis
    • Ohkama-Ohtsu, N., Zhao, P., Xiang, C., and Oliver, D. (2007b). Glutathione conjugates in the vacuole are degraded by gamma-glutamyl transpeptidase GGT3 in Arabidopsis. Plant J. 49: 878-888.
    • (2007) Plant J , vol.49 , pp. 878-888
    • Ohkama-Ohtsu, N.1    Zhao, P.2    Xiang, C.3    Oliver, D.4
  • 51
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • Rabeh, W.M., and Cook, P.F. (2004). Structure and mechanism of O-acetylserine sulfhydrylase. J. Biol. Chem. 279: 26803-26806.
    • (2004) J. Biol. Chem , vol.279 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 52
    • 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., Douce, R., and Ravanel, S. (2006). Methionine catabolism in Arabidopsis cells is initiated by a γ-cleavage process and leads to S-methylcysteine and isoleucine syntheses. Proc. Natl. Acad. Sci. USA 103: 15687-15692.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15687-15692
    • Rebeille, F.1    Jabrin, S.2    Bligny, R.3    Loizeau, K.4    Gambonnet, B.5    Van Wilder, V.6    Douce, R.7    Ravanel, S.8
  • 53
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • Reinders, J., Zahedi, R.P., Pfanner, N., Meisinger, C., and Sickmann, A. (2006). Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5: 1543-1554.
    • (2006) J. Proteome Res , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 54
    • 20444465757 scopus 로고    scopus 로고
    • Impact of reduced O-acetylserine(thiol)lyase isoform contents on potato plant metabolism
    • Riemenschneider, A., Riedel, K., Hoefgen, R., Papenbrock, J., and Hesse, H. (2005). Impact of reduced O-acetylserine(thiol)lyase isoform contents on potato plant metabolism. Plant Physiol. 137: 892-900.
    • (2005) Plant Physiol , vol.137 , pp. 892-900
    • Riemenschneider, A.1    Riedel, K.2    Hoefgen, R.3    Papenbrock, J.4    Hesse, H.5
  • 55
    • 0028893483 scopus 로고
    • Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform
    • Ruffet, M.L., Lebrun, M., Droux, M., and Douce, R. (1995). Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform. Eur. J. Biochem. 227: 500-509.
    • (1995) Eur. J. Biochem , vol.227 , pp. 500-509
    • Ruffet, M.L.1    Lebrun, M.2    Droux, M.3    Douce, R.4
  • 56
    • 16544394266 scopus 로고    scopus 로고
    • Sulfur assimilatory metabolism. The long and smelling road
    • Saito, K. (2004). Sulfur assimilatory metabolism. The long and smelling road. Plant Physiol. 136: 2443-2450.
    • (2004) Plant Physiol , vol.136 , pp. 2443-2450
    • Saito, K.1
  • 58
    • 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. (2004). Overproduction of SAT and/or OASTL in transgenic plants: A survey of effects. J. Exp. Bot. 55: 1881-1888.
    • (2004) J. Exp. Bot , vol.55 , pp. 1881-1888
    • Sirko, A.1    Blaszczyk, A.2    Liszewska, F.3
  • 59
    • 0000734956 scopus 로고
    • Studies of L-cysteine biosynthetic enzymes in Phaseolus vulgaris L
    • Smith, I.K. (1972). Studies of L-cysteine biosynthetic enzymes in Phaseolus vulgaris L. Plant Physiol. 50: 477-479.
    • (1972) Plant Physiol , vol.50 , pp. 477-479
    • Smith, I.K.1
  • 61
    • 57749112601 scopus 로고    scopus 로고
    • Regulation of gene expression in yeast sulphur metabolism
    • W.J. Cram, L.J. De Kok, I. Stulen, C. Brunold, and H. Rennenberg, eds Leiden, The Netherlands: Backhuys Publishers, pp
    • Thomas, D., Kuras, L., Cherest, H., Blaiseau, P.L., and Surdin-Kerjan, Y. (1997). Regulation of gene expression in yeast sulphur metabolism. In Sulphur Metabolism in Higher Plants, W.J. Cram, L.J. De Kok, I. Stulen, C. Brunold, and H. Rennenberg, eds (Leiden, The Netherlands: Backhuys Publishers), pp. 27-37.
    • (1997) Sulphur Metabolism in Higher Plants , pp. 27-37
    • Thomas, D.1    Kuras, L.2    Cherest, H.3    Blaiseau, P.L.4    Surdin-Kerjan, Y.5
  • 62
    • 1842504609 scopus 로고    scopus 로고
    • A novel high efficiency, low maintenance, hydroponic system for synchronous growth and flowering of Arabidopsis thaliana
    • Tocquin, P., Corbesier, L., Havelange, A., Pieltain, A., Kurtem, E., Bernier, G., and Perilleux, C. (2003). A novel high efficiency, low maintenance, hydroponic system for synchronous growth and flowering of Arabidopsis thaliana. BMC Plant Biol. 3: 2.
    • (2003) BMC Plant Biol , vol.3 , pp. 2
    • Tocquin, P.1    Corbesier, L.2    Havelange, A.3    Pieltain, A.4    Kurtem, E.5    Bernier, G.6    Perilleux, C.7
  • 63
    • 12744268500 scopus 로고    scopus 로고
    • Differential targeting of GSH1 and GSH2 is achieved by multiple transcription initiation: Implications for the compartmentation of glutathione biosynthesis in the Brassicaceae
    • Wachter, A., Wolf, S., Steininger, H., Bogs, J., and Rausch, T. (2005). Differential targeting of GSH1 and GSH2 is achieved by multiple transcription initiation: Implications for the compartmentation of glutathione biosynthesis in the Brassicaceae. Plant J. 41: 15-30.
    • (2005) Plant J , vol.41 , pp. 15-30
    • Wachter, A.1    Wolf, S.2    Steininger, H.3    Bogs, J.4    Rausch, T.5
  • 64
    • 0034121969 scopus 로고    scopus 로고
    • Cysteine synthase (O-acetylserine(thiol)lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase
    • Warrilow, A.G., and Hawkesford, M.J. (2000). Cysteine synthase (O-acetylserine(thiol)lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase. J. Exp. Bot. 51: 985-993.
    • (2000) J. Exp. Bot , vol.51 , pp. 985-993
    • Warrilow, A.G.1    Hawkesford, M.J.2
  • 65
    • 0034825333 scopus 로고    scopus 로고
    • The cysteine synthase complex from plants. Mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction
    • Wirtz, M., Berkowitz, O., Droux, M., and Hell, R. (2001). The cysteine synthase complex from plants. Mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction. Eur. J. Biochem. 268: 686-693.
    • (2001) Eur. J. Biochem , vol.268 , pp. 686-693
    • Wirtz, M.1    Berkowitz, O.2    Droux, M.3    Hell, R.4
  • 66
    • 29944437285 scopus 로고    scopus 로고
    • Synthesis of the sulfur amino acids: Cysteine and methionine
    • Wirtz, M., and Droux, M. (2005). Synthesis of the sulfur amino acids: Cysteine and methionine. Photosynth. Res. 86: 345-362.
    • (2005) Photosynth. Res , vol.86 , pp. 345-362
    • Wirtz, M.1    Droux, M.2
  • 67
    • 4344713150 scopus 로고    scopus 로고
    • O-Acetylserine(thiol)lyase: An enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana
    • Wirtz, M., Droux, M., and Hell, R. (2004). O-Acetylserine(thiol)lyase: An enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana. J. Exp. Bot. 55: 1785-1798.
    • (2004) J. Exp. Bot , vol.55 , pp. 1785-1798
    • Wirtz, M.1    Droux, M.2    Hell, R.3
  • 68
    • 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. (2003). Production of cysteine for bacterial and plant biotechnology: Application of cysteine feedback-insensitive isoforms of serine acetyltransferase. Amino Acids 24: 195-203.
    • (2003) Amino Acids , vol.24 , pp. 195-203
    • Wirtz, M.1    Hell, R.2
  • 69
    • 30944442063 scopus 로고    scopus 로고
    • Functional analysis of the cysteine synthase protein complex from plants: Structural, biochemical and regulatory properties
    • Wirtz, M., and Hell, R. (2006). Functional analysis of the cysteine synthase protein complex from plants: Structural, biochemical and regulatory properties. J. Plant Physiol. 163: 273-286.
    • (2006) J. Plant Physiol , vol.163 , pp. 273-286
    • Wirtz, M.1    Hell, R.2
  • 70
    • 34250665731 scopus 로고    scopus 로고
    • Dominant-negative modification reveals the regulatory function of the multimeric cysteine synthase protein complex in transgenic tobacco
    • Wirtz, M., and Hell, R. (2007). Dominant-negative modification reveals the regulatory function of the multimeric cysteine synthase protein complex in transgenic tobacco. Plant Cell 19: 625-639.
    • (2007) Plant Cell , vol.19 , pp. 625-639
    • Wirtz, M.1    Hell, R.2
  • 71
    • 0032011570 scopus 로고    scopus 로고
    • Purification and characterization of a novel cysteine synthase isozyme from spinach hydrated seeds
    • Yamaguchi, T., Zhu, X., and Masada, M. (1998). Purification and characterization of a novel cysteine synthase isozyme from spinach hydrated seeds. Biosci. Biotechnol. Biochem. 62: 501-507.
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 501-507
    • Yamaguchi, T.1    Zhu, X.2    Masada, M.3
  • 72
    • 0034074441 scopus 로고    scopus 로고
    • Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and β-cyanoalanine synthase
    • Yamaguchi, Y., Nakamura, T., Kusano, T., and Sano, H. (2000). Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and β-cyanoalanine synthase. Plant Cell Physiol. 41: 465-476.
    • (2000) Plant Cell Physiol , vol.41 , pp. 465-476
    • Yamaguchi, Y.1    Nakamura, T.2    Kusano, T.3    Sano, H.4
  • 73
    • 33646581753 scopus 로고    scopus 로고
    • Zhao, C., Kumada, Y., Imanaka, H., Imamura, K., and Nakanishi, K. (2006). Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli. Protein Expr. Purif. 47: 607-613.
    • Zhao, C., Kumada, Y., Imanaka, H., Imamura, K., and Nakanishi, K. (2006). Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli. Protein Expr. Purif. 47: 607-613.
  • 74
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmermann, P., Hirsch-Hoffmann, M., Hennig, L., and Gruissem, W. (2004). GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136: 2621-2632.
    • (2004) Plant Physiol , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


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