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Volumn 18, Issue 11, 2006, Pages 3088-3105

Arabidopsis SAMT1 defines a plastid transporter regulating plastid biogenesis and plant development

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; GENES; PLANT CELL CULTURE; PLANTS (BOTANY);

EID: 33845790059     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.040741     Document Type: Article
Times cited : (95)

References (98)
  • 1
    • 0013563765 scopus 로고
    • Regulation of threonine biosynthesis in barley seedlings (Hordeum vulgare L)
    • Aarnes, H. (1978). Regulation of threonine biosynthesis in barley seedlings (Hordeum vulgare L). Planta 140, 185-192.
    • (1978) Planta , vol.140 , pp. 185-192
    • Aarnes, H.1
  • 2
    • 1842844280 scopus 로고    scopus 로고
    • Identification of the human mitochondrial S-adenosylmethionine transporter: Bacterial expression, reconstitution, functional characterization and tissue distribution
    • Agrimi, G., Di Noia, M.A., Marobbio, C.M., Fiermonte, G., Lasorsa, F.M., and Palmieri, F. (2004). Identification of the human mitochondrial S-adenosylmethionine transporter: Bacterial expression, reconstitution, functional characterization and tissue distribution. Biochem. J. 379, 183-190.
    • (2004) Biochem. J. , vol.379 , pp. 183-190
    • Agrimi, G.1    Di Noia, M.A.2    Marobbio, C.M.3    Fiermonte, G.4    Lasorsa, F.M.5    Palmieri, F.6
  • 3
    • 12844280123 scopus 로고    scopus 로고
    • Tobacco Mg protoporphyrin IX methyltransferase is involved in inverse activation of Mg porphyrin and protoheme synthesis
    • Alawady, A.E., and Grimm, B. (2005). Tobacco Mg protoporphyrin IX methyltransferase is involved in inverse activation of Mg porphyrin and protoheme synthesis. Plant J. 41, 282-290.
    • (2005) Plant J. , vol.41 , pp. 282-290
    • Alawady, A.E.1    Grimm, B.2
  • 4
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., et al. (2003). Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301, 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1
  • 6
    • 0037076436 scopus 로고    scopus 로고
    • Carbocyclic fatty acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida
    • Bao, X., Katz, S., Pollard, M., and Ohlrogge, J. (2002). Carbocyclic fatty acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida. Proc. Natl. Acad. Sci. USA 99, 7172-7177.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7172-7177
    • Bao, X.1    Katz, S.2    Pollard, M.3    Ohlrogge, J.4
  • 7
    • 0038305971 scopus 로고    scopus 로고
    • Characterization of cyclopropane fatty-acid synthase from Sterculia foetida
    • Bao, X., Thelen, J.J., Bonaventure, G., and Ohlrogge, J.B. (2003). Characterization of cyclopropane fatty-acid synthase from Sterculia foetida. J. Biol. Chem. 278, 12846-12853.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12846-12853
    • Bao, X.1    Thelen, J.J.2    Bonaventure, G.3    Ohlrogge, J.B.4
  • 8
    • 77957008784 scopus 로고
    • Quinones in algae and higher plants
    • Barr, R., and Crane, F.L. (1971). Quinones in algae and higher plants. Methods Enzymol. 23, 372-408.
    • (1971) Methods Enzymol. , vol.23 , pp. 372-408
    • Barr, R.1    Crane, F.L.2
  • 9
    • 27144449733 scopus 로고    scopus 로고
    • Folate metabolism in plants: An Arabidopsis homolog of the mammalian mitochondrial folate transporter mediates folate import into chloroplasts
    • Bedhomme, M., Hoffmann, M., McCarthy, E.A., Gambonnet, B., Moran, R.G., Rebeille, F., and Ravanel, S. (2005). Folate metabolism in plants: An Arabidopsis homolog of the mammalian mitochondrial folate transporter mediates folate import into chloroplasts. J. Biol. Chem. 280, 34823-34831.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34823-34831
    • Bedhomme, M.1    Hoffmann, M.2    McCarthy, E.A.3    Gambonnet, B.4    Moran, R.G.5    Rebeille, F.6    Ravanel, S.7
  • 10
    • 0023655363 scopus 로고
    • Light-regulated methylation of chloroplast proteins
    • Black, M.T., Meyer, D., Widger, W.R., and Cramer, W.A. (1987). Light-regulated methylation of chloroplast proteins. J. Biol. Chem. 262, 9803-9807.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9803-9807
    • Black, M.T.1    Meyer, D.2    Widger, W.R.3    Cramer, W.A.4
  • 11
    • 0036153918 scopus 로고    scopus 로고
    • The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes
    • Block, M.A., Tewari, A.K., Albrieux, C., Marechal, E., and Joyard, J. (2002). The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes. Eur. J. Biochem. 269, 240-248.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 240-248
    • Block, M.A.1    Tewari, A.K.2    Albrieux, C.3    Marechal, E.4    Joyard, J.5
  • 12
    • 0028520248 scopus 로고
    • Distinct phenotypes generated by overexpression and suppression of S-adenosyl-L-methionine synthetase reveal developmental patterns of gene silencing in tobacco
    • Boerjan, W., Bauw, G., Van Montagu, M., and Inze, D. (1994). Distinct phenotypes generated by overexpression and suppression of S-adenosyl-L- methionine synthetase reveal developmental patterns of gene silencing in tobacco. Plant Cell 6, 1401-1414.
    • (1994) Plant Cell , vol.6 , pp. 1401-1414
    • Boerjan, W.1    Bauw, G.2    Van Montagu, M.3    Inze, D.4
  • 13
    • 0032132839 scopus 로고    scopus 로고
    • Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits
    • Bouvier, F., d'Harlingue, A., Suire, C., Backhaus, R.A., and Camara, B. (1998). Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits. Plant Physiol. 117, 1423-1431.
    • (1998) Plant Physiol. , vol.117 , pp. 1423-1431
    • Bouvier, F.1    D'Harlingue, A.2    Suire, C.3    Backhaus, R.A.4    Camara, B.5
  • 14
    • 27744577599 scopus 로고    scopus 로고
    • Biogenesis, molecular regulation and function of plant isoprenoids
    • Bouvier, F., Rahier, A., and Camara, B. (2005). Biogenesis, molecular regulation and function of plant isoprenoids. Prog. Lipid Res. 44, 357-429.
    • (2005) Prog. Lipid Res. , vol.44 , pp. 357-429
    • Bouvier, F.1    Rahier, A.2    Camara, B.3
  • 15
    • 0346664458 scopus 로고    scopus 로고
    • Oxidative remodeling of chromoplast carotenoids: Identification of the carotenoid dioxygenase CsCCD and CsZCD genes involved in Crocus secondary metabolite biogenesis
    • Bouvier, F., Suire, C., Mutterer, J., and Camara, B. (2003). Oxidative remodeling of chromoplast carotenoids: Identification of the carotenoid dioxygenase CsCCD and CsZCD genes involved in Crocus secondary metabolite biogenesis. Plant Cell 15, 47-62.
    • (2003) Plant Cell , vol.15 , pp. 47-62
    • Bouvier, F.1    Suire, C.2    Mutterer, J.3    Camara, B.4
  • 16
    • 0032533305 scopus 로고    scopus 로고
    • Measurement of plasma S-adenosylmethionine and S-adenosylhomocysteine as their fluorescent isoindoles
    • Capdevila, A., and Wagner, C. (1998). Measurement of plasma S-adenosylmethionine and S-adenosylhomocysteine as their fluorescent isoindoles. Anal. Biochem. 264, 180-184.
    • (1998) Anal. Biochem. , vol.264 , pp. 180-184
    • Capdevila, A.1    Wagner, C.2
  • 17
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998). Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743.
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 18
    • 0032558460 scopus 로고    scopus 로고
    • Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine
    • Curien, G., Job, D., Douce, R., and Dumas, R. (1998). Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine. Biochemistry 37, 13212-13221.
    • (1998) Biochemistry , vol.37 , pp. 13212-13221
    • Curien, G.1    Job, D.2    Douce, R.3    Dumas, R.4
  • 19
    • 20144365505 scopus 로고    scopus 로고
    • A decade of progress in understanding vitamin e synthesis in plants
    • DellaPenna, D. (2005). A decade of progress in understanding vitamin E synthesis in plants. J. Plant Physiol. 162, 729-737.
    • (2005) J. Plant Physiol. , vol.162 , pp. 729-737
    • Dellapenna, D.1
  • 20
    • 0022372814 scopus 로고
    • Plastid enzymes of terpenoid biosynthesis. Purification and characterization of γ-tocopherol methyltransferase from Capsicum chromoplasts
    • d'Harlingue, A., and Camara, B. (1985). Plastid enzymes of terpenoid biosynthesis. Purification and characterization of γ-tocopherol methyltransferase from Capsicum chromoplasts. J. Biol. Chem. 260, 15200-15203.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15200-15203
    • D'Harlingue, A.1    Camara, B.2
  • 21
    • 33845771085 scopus 로고
    • La méthionine adénosyltransférase des végétaux: Mise en évidence de 3 formes
    • Dogbo, O., and Camara, B. (1986). La méthionine adénosyltransférase des végétaux: Mise en évidence de 3 formes. C. R. Acad. Sci. Paris III 303, 93-96.
    • (1986) C. R. Acad. Sci. Paris III , vol.303 , pp. 93-96
    • Dogbo, O.1    Camara, B.2
  • 23
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and von Heijne, G. (2000). Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300, 1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 24
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G. (1999). ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8, 978-984.
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 25
    • 0037431024 scopus 로고    scopus 로고
    • Constitutive overexpression of barley 4-hydroxyphenylpyruvate dioxygenase in tobacco results in elevation of the vitamin E content in seeds but not in leaves
    • Falk, J., Andersen, G., Kernebeck, B., and Krupinska, K. (2003). Constitutive overexpression of barley 4-hydroxyphenylpyruvate dioxygenase in tobacco results in elevation of the vitamin E content in seeds but not in leaves. FEBS Lett. 540, 35-40.
    • (2003) FEBS Lett. , vol.540 , pp. 35-40
    • Falk, J.1    Andersen, G.2    Kernebeck, B.3    Krupinska, K.4
  • 28
    • 0031105611 scopus 로고    scopus 로고
    • A new class of plastidic phosphate translocators: A putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter
    • Fischer, K., Kammerer, B., Gutensohn, M., Arbinger, B., Weber, A., Hausler, R.E., and Flugge, U.I. (1997). A new class of plastidic phosphate translocators: A putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter. Plant Cell 9, 453-462.
    • (1997) Plant Cell , vol.9 , pp. 453-462
    • Fischer, K.1    Kammerer, B.2    Gutensohn, M.3    Arbinger, B.4    Weber, A.5    Hausler, R.E.6    Flugge, U.I.7
  • 29
    • 0034895894 scopus 로고    scopus 로고
    • A method for isolating a high yield of Arabidopsis chloroplasts capable of efficient import of precursor proteins
    • Fitzpatrick, L.M., and Keegstra, K. (2001). A method for isolating a high yield of Arabidopsis chloroplasts capable of efficient import of precursor proteins. Plant J. 27, 59-65.
    • (2001) Plant J. , vol.27 , pp. 59-65
    • Fitzpatrick, L.M.1    Keegstra, K.2
  • 30
    • 0024574552 scopus 로고
    • The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: Nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts
    • Flügge, U.I., Fischer, K., Gross, A., Sebald, W., Lottspeich, F., and Eckerskorn, C. (1989). The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: Nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts. EMBO J. 8, 39-46.
    • (1989) EMBO J. , vol.8 , pp. 39-46
    • Flügge, U.I.1    Fischer, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 31
    • 0028155460 scopus 로고
    • A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues
    • Flügge, U.I., and Weber, A. (1994). A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues. Planta 194, 181-185.
    • (1994) Planta , vol.194 , pp. 181-185
    • Flügge, U.I.1    Weber, A.2
  • 32
    • 2342631335 scopus 로고    scopus 로고
    • S-Adenosylmethionine: Nothing goes to waste
    • Fontecave, M., Atta, M., and Mulliez, E. (2004). S-Adenosylmethionine: Nothing goes to waste. Trends Biochem. Sci. 29, 243-249.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 243-249
    • Fontecave, M.1    Atta, M.2    Mulliez, E.3
  • 33
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A.L., Fowler, S., and Lazarow, P.B. (1982). Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 93, 97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 34
    • 0028833955 scopus 로고
    • Regulation of lysine and threonine synthesis
    • Galili, G. (1995). Regulation of lysine and threonine synthesis. Plant Cell 7, 899-906.
    • (1995) Plant Cell , vol.7 , pp. 899-906
    • Galili, G.1
  • 35
    • 0036331751 scopus 로고    scopus 로고
    • Metabolic engineering of amino acids and storage proteins in plants
    • Galili, G., and Hofgen, R. (2002). Metabolic engineering of amino acids and storage proteins in plants. Metab. Eng. 4, 3-11.
    • (2002) Metab. Eng. , vol.4 , pp. 3-11
    • Galili, G.1    Hofgen, R.2
  • 36
    • 0001636206 scopus 로고
    • Regulatory structure of the biosynthetic pathway for the aspartate family of amino acids in Lemna paucicostata Hegelm. 6746, with special reference to the role of aspartokinase
    • Giovanelli, J., Mudd, S.H., and Dakto, A.H. (1989). Regulatory structure of the biosynthetic pathway for the aspartate family of amino acids in Lemna paucicostata Hegelm. 6746, with special reference to the role of aspartokinase. Plant Physiol. 90, 1584-1599.
    • (1989) Plant Physiol. , vol.90 , pp. 1584-1599
    • Giovanelli, J.1    Mudd, S.H.2    Dakto, A.H.3
  • 38
    • 0025336798 scopus 로고
    • Analysis of pre-mRNA processing in transfected plant protoplasts
    • Goodall, G.J., Wiebauer, K., and Filipowicz, W. (1990). Analysis of pre-mRNA processing in transfected plant protoplasts. Methods Enzymol. 181, 148-161.
    • (1990) Methods Enzymol. , vol.181 , pp. 148-161
    • Goodall, G.J.1    Wiebauer, K.2    Filipowicz, W.3
  • 39
    • 0031587020 scopus 로고    scopus 로고
    • Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts
    • Grimm, R., Grimm, M., Eckerskorn, C., Pohlmeyer, K., Rohl, T., and Soll, J. (1997). Postimport methylation of the small subunit of ribulose-1,5- bisphosphate carboxylase in chloroplasts. FEBS Lett. 408, 350-354.
    • (1997) FEBS Lett. , vol.408 , pp. 350-354
    • Grimm, R.1    Grimm, M.2    Eckerskorn, C.3    Pohlmeyer, K.4    Rohl, T.5    Soll, J.6
  • 40
    • 0000023327 scopus 로고
    • Comparison of the kinetic properties, inhibition and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts
    • Gross, A., Brückner, G., Heldt, H.W., and Flügge, U.I. (1990). Comparison of the kinetic properties, inhibition and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts. Planta 180, 262-271.
    • (1990) Planta , vol.180 , pp. 262-271
    • Gross, A.1    Brückner, G.2    Heldt, H.W.3    Flügge, U.I.4
  • 42
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood, J.L., Tonti-Filippini, J., Verboom, R.E., and Millar, A.H. (2005). Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol. 139, 598-609.
    • (2005) Plant Physiol. , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 43
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A.B., and Tsien, R.Y. (1995). Improved green fluorescence. Nature 373, 663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 44
    • 0000638213 scopus 로고
    • Measurement of metabolite movement across the envelope and of the pH in the stroma and the thylakoid space in intact chloroplasts
    • Heldt, H.W. (1980). Measurement of metabolite movement across the envelope and of the pH in the stroma and the thylakoid space in intact chloroplasts. Methods Enzymol. 69, 604-613.
    • (1980) Methods Enzymol. , vol.69 , pp. 604-613
    • Heldt, H.W.1
  • 45
    • 0033764485 scopus 로고    scopus 로고
    • The chloroplast and leaf developmental mutant, pale cress, exhibits light-conditional severity and symptoms characteristic of its ABA deficiency
    • Holding, D.R., Springer, P.S., and Coomber, S.A. (2000). The chloroplast and leaf developmental mutant, pale cress, exhibits light-conditional severity and symptoms characteristic of its ABA deficiency. Ann. Bot. (Lond.) 86, 953-962.
    • (2000) Ann. Bot. (Lond.) , vol.86 , pp. 953-962
    • Holding, D.R.1    Springer, P.S.2    Coomber, S.A.3
  • 46
    • 0031571158 scopus 로고    scopus 로고
    • Transport of S-adenosylmethionine in isolated rat liver mitochondria
    • Horne, D.W., Holloway, R.S., and Wagner, C. (1997). Transport of S-adenosylmethionine in isolated rat liver mitochondria. Arch. Biochem. Biophys. 343, 201-206.
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 201-206
    • Horne, D.W.1    Holloway, R.S.2    Wagner, C.3
  • 47
    • 0017688926 scopus 로고
    • Reconstitution and purification of the D-glucose transporter from human erythrocytes
    • Kasahara, M., and Hinkle, P.C. (1977). Reconstitution and purification of the D-glucose transporter from human erythrocytes. J. Biol. Chem. 252, 7384-7390.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7384-7390
    • Kasahara, M.1    Hinkle, P.C.2
  • 48
    • 0036274678 scopus 로고    scopus 로고
    • Ethylene biosynthesis and signaling networks
    • Kevin, L.I., Wang, C., Li, H., and Ecker, J.R. (2002). Ethylene biosynthesis and signaling networks. Plant Cell 14 (suppl.), S131-S151.
    • (2002) Plant Cell , vol.14 , Issue.SUPPL.
    • Kevin, L.I.1    Wang, C.2    Li, H.3    Ecker, J.R.4
  • 50
    • 0037221149 scopus 로고    scopus 로고
    • Characterization of gamma-tocopherol methyltransferases from Capsicum annuum L and Arabidopsis thaliana
    • Koch, M., Lemke, R., Heise, K.P., and Mock, H.P. (2003). Characterization of gamma-tocopherol methyltransferases from Capsicum annuum L and Arabidopsis thaliana. Eur. J. Biochem. 270, 84-92.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 84-92
    • Koch, M.1    Lemke, R.2    Heise, K.P.3    Mock, H.P.4
  • 51
    • 0036800808 scopus 로고    scopus 로고
    • The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles
    • Koo, A.J., and Ohlrogge, J.B. (2002). The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles. Plant Physiol. 130, 823-836.
    • (2002) Plant Physiol. , vol.130 , pp. 823-836
    • Koo, A.J.1    Ohlrogge, J.B.2
  • 54
    • 0032077269 scopus 로고    scopus 로고
    • Functional integration of non-native carotenoids into chloroplasts by viral-derived expression of capsanthin-capsorubin synthase in Nicotiana benthamiana
    • Kumagai, M.H., Keller, Y., Bouvier, F., Clary, D., and Camara, B. (1998). Functional integration of non-native carotenoids into chloroplasts by viral-derived expression of capsanthin-capsorubin synthase in Nicotiana benthamiana. Plant J. 14, 305-315.
    • (1998) Plant J. , vol.14 , pp. 305-315
    • Kumagai, M.H.1    Keller, Y.2    Bouvier, F.3    Clary, D.4    Camara, B.5
  • 55
    • 0034989707 scopus 로고    scopus 로고
    • Amitrole treatment of etiolated barley seedlings leads to deregulation of tetrapyrrole synthesis and to reduced expression of Lhc and RbcS genes
    • La Rocca, N., Rascio, N., Oster, U., and Rudiger, W. (2001). Amitrole treatment of etiolated barley seedlings leads to deregulation of tetrapyrrole synthesis and to reduced expression of Lhc and RbcS genes. Planta 213, 101-108.
    • (2001) Planta , vol.213 , pp. 101-108
    • La Rocca, N.1    Rascio, N.2    Oster, U.3    Rudiger, W.4
  • 56
    • 24044480332 scopus 로고    scopus 로고
    • Identification and characterization of a novel plastidic adenine nucleotide uniporter from Solanum tuberosum
    • Leroch, M., Kirchberger, S., Haferkamp, I., Wahl, M., Neuhaus, H.E., and Tjaden, J. (2005). Identification and characterization of a novel plastidic adenine nucleotide uniporter from Solanum tuberosum. J. Biol. Chem. 280, 17992-18000.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17992-18000
    • Leroch, M.1    Kirchberger, S.2    Haferkamp, I.3    Wahl, M.4    Neuhaus, H.E.5    Tjaden, J.6
  • 57
    • 0027411773 scopus 로고
    • Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step
    • Loddenkotter, B., Kammerer, B., Fischer, K., and Flügge, U.I. (1993). Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step. Proc. Natl. Acad. Sci. USA 90, 2155-2159.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2155-2159
    • Loddenkotter, B.1    Kammerer, B.2    Fischer, K.3    Flügge, U.I.4
  • 58
    • 0017183716 scopus 로고
    • Threonine synthetase from higher plants: Stimulation by S-adenosylmethionine and inhibition by cysteine
    • Madison, J.T., and Thompson, J.F. (1976). Threonine synthetase from higher plants: Stimulation by S-adenosylmethionine and inhibition by cysteine. Biochem. Biophys. Res. Commun. 71, 684-691.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 684-691
    • Madison, J.T.1    Thompson, J.F.2
  • 59
    • 0027287947 scopus 로고
    • Plants that express a potyvirus proteinase gene are resistant to virus infection
    • Maiti, I.B., Murphy, J.F., Shaw, J.G., and Hunt, A.G. (1993). Plants that express a potyvirus proteinase gene are resistant to virus infection. Proc. Natl. Acad. Sci. USA 90, 6110-6114.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6110-6114
    • Maiti, I.B.1    Murphy, J.F.2    Shaw, J.G.3    Hunt, A.G.4
  • 60
    • 0344442851 scopus 로고    scopus 로고
    • Identification and functional reconstitution of yeast mitochondrial carrier for S-adenosylmethionine
    • Marobbio, C.M., Agrimi, G., Lasorsa, F.M., and Palmieri, F. (2003). Identification and functional reconstitution of yeast mitochondrial carrier for S-adenosylmethionine. EMBO J. 22, 5975-5982.
    • (2003) EMBO J. , vol.22 , pp. 5975-5982
    • Marobbio, C.M.1    Agrimi, G.2    Lasorsa, F.M.3    Palmieri, F.4
  • 61
    • 0027143463 scopus 로고
    • Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension cultures
    • May, M.J., and Leaver, C.J. (1993). Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension cultures. Plant Physiol. 103, 621-627.
    • (1993) Plant Physiol. , vol.103 , pp. 621-627
    • May, M.J.1    Leaver, C.J.2
  • 62
  • 64
    • 0035687541 scopus 로고    scopus 로고
    • Sustaining S-adenosyl-L-methionine-dependent methyltransferase activity in plant cells
    • Moffatt, B.A., and Weretilnyk, E.A. (2001). Sustaining S-adenosyl-L-methionine-dependent methyltransferase activity in plant cells. Physiol. Plant. 113, 435-442.
    • (2001) Physiol. Plant. , vol.113 , pp. 435-442
    • Moffatt, B.A.1    Weretilnyk, E.A.2
  • 65
    • 0001037512 scopus 로고
    • Chlorophyll determination in intact tissues using N,N-dimethylformamide
    • Moran, R., and Porath, D. (1980). Chlorophyll determination in intact tissues using N,N-dimethylformamide. Plant Physiol. 65, 478-479.
    • (1980) Plant Physiol. , vol.65 , pp. 478-479
    • Moran, R.1    Porath, D.2
  • 66
    • 0038468471 scopus 로고    scopus 로고
    • Functional analysis of the 37 kDa inner envelope membrane polypeptide in chloroplast biogenesis using a Ds-tagged Arabidopsis pale-green mutant
    • Motohashi, R., Ito, T., Kobayashi, M., Taji, T., Nagata, N., Asami, T., Yoshida, S., Yamaguchi-Shinozaki, K., and Shinozaki, K. (2003). Functional analysis of the 37 kDa inner envelope membrane polypeptide in chloroplast biogenesis using a Ds-tagged Arabidopsis pale-green mutant. Plant J. 34, 719-731.
    • (2003) Plant J. , vol.34 , pp. 719-731
    • Motohashi, R.1    Ito, T.2    Kobayashi, M.3    Taji, T.4    Nagata, N.5    Asami, T.6    Yoshida, S.7    Yamaguchi-Shinozaki, K.8    Shinozaki, K.9
  • 67
    • 0035115575 scopus 로고    scopus 로고
    • Subcellular compartmentation of the diterpene carnosic acid and its derivatives in the leaves of rosemary
    • Munne-Bosch, S., and Alegre, L. (2001). Subcellular compartmentation of the diterpene carnosic acid and its derivatives in the leaves of rosemary. Plant Physiol. 125, 1094-1102.
    • (2001) Plant Physiol. , vol.125 , pp. 1094-1102
    • Munne-Bosch, S.1    Alegre, L.2
  • 68
    • 0037197978 scopus 로고    scopus 로고
    • A chloroplast-resident DNA methyltransferase is responsible for hypermethylation of chloroplast genes in Chlamydomonas maternal gametes
    • Nishiyama, R., Ito, M., Yamaguchi, Y., Koizumi, N., and Sano, H. (2002). A chloroplast-resident DNA methyltransferase is responsible for hypermethylation of chloroplast genes in Chlamydomonas maternal gametes. Proc. Natl. Acad. Sci. USA 99, 5925-5930.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5925-5930
    • Nishiyama, R.1    Ito, M.2    Yamaguchi, Y.3    Koizumi, N.4    Sano, H.5
  • 69
    • 0035903573 scopus 로고    scopus 로고
    • Identification and functional reconstitution of the yeast peroxisomal adenine nucleotide transporter
    • Palmieri, L., Rottensteiner, H., Girzalsky, W., Scarcia, P., Palmieri, F., and Erdmann, R. (2001). Identification and functional reconstitution of the yeast peroxisomal adenine nucleotide transporter. EMBO J. 20, 5049-5059.
    • (2001) EMBO J. , vol.20 , pp. 5049-5059
    • Palmieri, L.1    Rottensteiner, H.2    Girzalsky, W.3    Scarcia, P.4    Palmieri, F.5    Erdmann, R.6
  • 70
    • 0001456147 scopus 로고
    • Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli
    • Paulsen, H., Rümler, W., and Rüdiger, W. (1990). Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli. Planta 181, 204-211.
    • (1990) Planta , vol.181 , pp. 204-211
    • Paulsen, H.1    Rümler, W.2    Rüdiger, W.3
  • 71
    • 0016716820 scopus 로고
    • Specificity and genetics of S-adenosylmethionine transport in Saccharomyces cerevisiae
    • Petrotta-Simpson, T.F., Tamaldge, J.E., and Spence, K.D. (1975). Specificity and genetics of S-adenosylmethionine transport in Saccharomyces cerevisiae. J. Bacteriol. 123, 516-522.
    • (1975) J. Bacteriol. , vol.123 , pp. 516-522
    • Petrotta-Simpson, T.F.1    Tamaldge, J.E.2    Spence, K.D.3
  • 72
    • 1542350574 scopus 로고    scopus 로고
    • The growing family of mitochondrial carriers in Arabidopsis
    • Picault, N., Hodges, M., Palmieri, L., and Palmieri, F. (2004). The growing family of mitochondrial carriers in Arabidopsis. Trends Plant Sci. 9, 138-146.
    • (2004) Trends Plant Sci. , vol.9 , pp. 138-146
    • Picault, N.1    Hodges, M.2    Palmieri, L.3    Palmieri, F.4
  • 73
    • 0000913635 scopus 로고
    • Transmethylation and demethylation reactions in the metabolism of secondary plant products
    • E.E. Conn, ed (New York: Academic Press)
    • Poulton, J.E. (1981). Transmethylation and demethylation reactions in the metabolism of secondary plant products. In The Biochemistry of Plants, E.E. Conn, ed (New York: Academic Press), pp. 667-723.
    • (1981) The Biochemistry of Plants , pp. 667-723
    • Poulton, J.E.1
  • 74
    • 2542430082 scopus 로고    scopus 로고
    • Methionine metabolism in plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol
    • Ravanel, S., Block, M.A., Rippert, P., Jabrin, S., Curien, G., Rebeille, F., and Douce, R. (2004). Methionine metabolism in plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol. J. Biol. Chem. 279, 22548-22557.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22548-22557
    • Ravanel, S.1    Block, M.A.2    Rippert, P.3    Jabrin, S.4    Curien, G.5    Rebeille, F.6    Douce, R.7
  • 75
    • 0043067995 scopus 로고    scopus 로고
    • The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2
    • Renne, P., Dressen, U., Hebbeker, U., Hille, D., Flugge, U.I., Westhoff, P., and Weber, A.P. (2003). The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2. Plant J. 35, 316-331.
    • (2003) Plant J. , vol.35 , pp. 316-331
    • Renne, P.1    Dressen, U.2    Hebbeker, U.3    Hille, D.4    Flugge, U.I.5    Westhoff, P.6    Weber, A.P.7
  • 76
    • 0033214492 scopus 로고    scopus 로고
    • Transport of sulfonium compounds. Characterization of the S-adenosylmethionine and S-methylmethionine permeases from the yeast Saccharomyces cerevisiae
    • Rouillon, A., Surdin-Kerjan, Y., and Thomas, D. (1999). Transport of sulfonium compounds. Characterization of the S-adenosylmethionine and S-methylmethionine permeases from the yeast Saccharomyces cerevisiae. J. Biol. Chem. 274, 28096-28105.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28096-28105
    • Rouillon, A.1    Surdin-Kerjan, Y.2    Thomas, D.3
  • 80
    • 0036008585 scopus 로고    scopus 로고
    • High free-methionine and decreased lignin content result from a mutation in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene
    • Shen, B., Li, C., and Tarczynski, M.C. (2002). High free-methionine and decreased lignin content result from a mutation in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene. Plant J. 29, 371-380.
    • (2002) Plant J. , vol.29 , pp. 371-380
    • Shen, B.1    Li, C.2    Tarczynski, M.C.3
  • 81
    • 0038076101 scopus 로고    scopus 로고
    • Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803
    • Shepherd, M., Reid, J.D., and Hunter, C.N. (2003). Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803. Biochem. J. 371, 351-360.
    • (2003) Biochem. J. , vol.371 , pp. 351-360
    • Shepherd, M.1    Reid, J.D.2    Hunter, C.N.3
  • 82
    • 0032509317 scopus 로고    scopus 로고
    • Elevating the vitamin e content of plants through metabolic engineering
    • Shintani, D., and DellaPenna, D. (1998). Elevating the vitamin E content of plants through metabolic engineering. Science 282, 2098-2100.
    • (1998) Science , vol.282 , pp. 2098-2100
    • Shintani, D.1    DellaPenna, D.2
  • 84
    • 0347927268 scopus 로고    scopus 로고
    • Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrinIX
    • Strand, A., Asami, T., Alonso, J., Ecker, J.R., and Chory, J. (2003). Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrinIX. Nature 421, 79-83.
    • (2003) Nature , vol.421 , pp. 79-83
    • Strand, A.1    Asami, T.2    Alonso, J.3    Ecker, J.R.4    Chory, J.5
  • 85
    • 0033197510 scopus 로고    scopus 로고
    • The phosphoenolpyruvate/phosphate translocator is required for phenolic metabolism, palisade cell development, and plastid-dependent nuclear gene expression
    • Streatfield, S.J., Weber, A., Kinsman, E.A., Hausler, R.E., Li, J., Post-Beittenmiller, D., Kaiser, W.M., Pyke, K.A., Flugge, U.I., and Chory, J. (1999). The phosphoenolpyruvate/phosphate translocator is required for phenolic metabolism, palisade cell development, and plastid-dependent nuclear gene expression. Plant Cell 11, 1609-1622.
    • (1999) Plant Cell , vol.11 , pp. 1609-1622
    • Streatfield, S.J.1    Weber, A.2    Kinsman, E.A.3    Hausler, R.E.4    Li, J.5    Post-Beittenmiller, D.6    Kaiser, W.M.7    Pyke, K.A.8    Flugge, U.I.9    Chory, J.10
  • 86
    • 0028980954 scopus 로고
    • The maize brittle1 gene encodes amyloplast membrane polypeptides
    • Sullivan, T.D., and Kaneko, Y. (1995). The maize brittle1 gene encodes amyloplast membrane polypeptides. Planta 196, 477-484.
    • (1995) Planta , vol.196 , pp. 477-484
    • Sullivan, T.D.1    Kaneko, Y.2
  • 87
    • 0038419637 scopus 로고    scopus 로고
    • Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    • Trievel, R.C., Flynn, E.M., Houtz, R.L., and Hurley, J.H. (2003). Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nat. Struct. Biol. 10, 545-552.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 545-552
    • Trievel, R.C.1    Flynn, E.M.2    Houtz, R.L.3    Hurley, J.H.4
  • 88
    • 0038643374 scopus 로고    scopus 로고
    • S-Adenosylmethionine transport in Rickettsia prowazekii
    • Tucker, A.M., Winkler, H.H., Driskell, L.O., and Wood, D.O. (2003). S-Adenosylmethionine transport in Rickettsia prowazekii. J. Bacteriol. 185, 3031-3035.
    • (2003) J. Bacteriol. , vol.185 , pp. 3031-3035
    • Tucker, A.M.1    Winkler, H.H.2    Driskell, L.O.3    Wood, D.O.4
  • 89
    • 0000087176 scopus 로고
    • Intracellular localization of aspartate kinase and the enzymes of threonine and methionine biosynthesis in green leaves
    • Wallsgrove, R.M., Lea, P.J., and Miflin, B.J. (1983). Intracellular localization of aspartate kinase and the enzymes of threonine and methionine biosynthesis in green leaves. Plant Physiol. 71, 780-784.
    • (1983) Plant Physiol. , vol.71 , pp. 780-784
    • Wallsgrove, R.M.1    Lea, P.J.2    Miflin, B.J.3
  • 90
    • 2442484711 scopus 로고    scopus 로고
    • Using mutants to probe the in vivo function of plastid envelope membrane metabolite transporters
    • Weber, A.P., Schneidereit, J., and Voll, L.M. (2004). Using mutants to probe the in vivo function of plastid envelope membrane metabolite transporters. J. Exp. Bot. 55, 1231-1244.
    • (2004) J. Exp. Bot. , vol.55 , pp. 1231-1244
    • Weber, A.P.1    Schneidereit, J.2    Voll, L.M.3
  • 91
    • 20444385506 scopus 로고    scopus 로고
    • Solute transporters of the plastid envelope membrane
    • Weber, A.P., Schwacke, R., and Flugge, U.I. (2005). Solute transporters of the plastid envelope membrane. Annu. Rev. Plant Biol. 56, 133-164.
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 133-164
    • Weber, A.P.1    Schwacke, R.2    Flugge, U.I.3
  • 92
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss, H., Friedrich, T., Hofhaus, G., and Preis, D. (1991). The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197, 563-576.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 93
    • 0007555497 scopus 로고
    • Analysis of pea chloroplast inner and outer envelope membrane proteins by two-dimensional gel electrophoresis and their comparison with stroma proteins
    • Werner-Washburne, M., Cline, K., and Keegstra, K. (1983). Analysis of pea chloroplast inner and outer envelope membrane proteins by two-dimensional gel electrophoresis and their comparison with stroma proteins. Plant Physiol. 73, 569-575.
    • (1983) Plant Physiol. , vol.73 , pp. 569-575
    • Werner-Washburne, M.1    Cline, K.2    Keegstra, K.3
  • 94
    • 0027976083 scopus 로고
    • Subcellular volumes and metabolite concentrations in spinach leaves
    • Winter, H., Robinson, D.G., and Heldt, H.W. (1994). Subcellular volumes and metabolite concentrations in spinach leaves. Planta 193, 530-535.
    • (1994) Planta , vol.193 , pp. 530-535
    • Winter, H.1    Robinson, D.G.2    Heldt, H.W.3
  • 95
    • 0033579564 scopus 로고    scopus 로고
    • Rubisco small and large subunit N-methyltransferases. Bi- and monofunctional methyltransferases that methylate the small and large subunits of Rubisco
    • Ying, Z., Mulligan, R.M., Janney, N., and Houtz, R.L. (1999). Rubisco small and large subunit N-methyltransferases. Bi- and monofunctional methyltransferases that methylate the small and large subunits of Rubisco. J. Biol. Chem. 274, 36750-36756.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36750-36756
    • Ying, Z.1    Mulligan, R.M.2    Janney, N.3    Houtz, R.L.4
  • 96
    • 0032190317 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit nepsilon-methyltransferase
    • Zheng, Q., Simel, E.J., Klein, P.E., Royer, M.T., and Houtz, R.L. (1998). Expression, purification, and characterization of recombinant ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit nepsilon-methyltransferase. Protein Expr. Purif. 14, 104-112.
    • (1998) Protein Expr. Purif. , vol.14 , pp. 104-112
    • Zheng, Q.1    Simel, E.J.2    Klein, P.E.3    Royer, M.T.4    Houtz, R.L.5
  • 97
    • 27244438560 scopus 로고    scopus 로고
    • Gene-expression analysis and network discovery using Genevestigator
    • Zimmermann, P., Hennig, L., and Gruissem, W. (2005). Gene-expression analysis and network discovery using Genevestigator. Trends Plant Sci. 10, 407-409.
    • (2005) Trends Plant Sci. , vol.10 , pp. 407-409
    • Zimmermann, P.1    Hennig, L.2    Gruissem, W.3
  • 98
    • 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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