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Volumn 47, Issue 5, 2006, Pages 613-621

Phosphoenolpyruvate carboxylase plays a crucial role in limiting nitrogen fixation in Lotus japonicus nodules

Author keywords

Carbon; Lotus japonicus; Nitrogen; Nodule; Phosphoenolpyruvate carboxylase

Indexed keywords

ACETYLENE; AMINOTRANSFERASE; CARBON DIOXIDE; GLUCOSYLTRANSFERASE; NITROGEN; NITROGENASE; PHOSPHOENOLPYRUVATE CARBOXYLASE; PLANT DNA; PLANT RNA; SERINE GLYOXYLATE AMINOTRANSFERASE; SERINE-GLYOXYLATE AMINOTRANSFERASE; SUCROSE SYNTHASE; VEGETABLE PROTEIN;

EID: 33745595881     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pcj028     Document Type: Article
Times cited : (44)

References (44)
  • 1
    • 77957181545 scopus 로고
    • Immunological studies of betaine aldehyde dehydrogenase in barley
    • Arakawa, K., Mizuno, K., Kishitani S. and Takabe, T. (1992). Immunological studies of betaine aldehyde dehydrogenase in barley. Plant Cell Physiol. 33: 833-840.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 833-840
    • Arakawa, K.1    Mizuno, K.2    Kishitani, S.3    Takabe, T.4
  • 2
    • 0030953665 scopus 로고    scopus 로고
    • Possible causes of the decline in soybean nitrogen fixation in the presence of nitrate
    • Arrese-Igor, C., Minchin, F.R., Gordon, A.J. and Nath, A.K. (1997) Possible causes of the decline in soybean nitrogen fixation in the presence of nitrate. J. Exp. Bot. 48: 905-914.
    • (1997) J. Exp. Bot. , vol.48 , pp. 905-914
    • Arrese-Igor, C.1    Minchin, F.R.2    Gordon, A.J.3    Nath, A.K.4
  • 3
    • 0003243361 scopus 로고
    • 2-Oxoglutarate
    • Edited by Bergmeyer, H.U. Verlag Chemie, Weinheim
    • Bergmeyer, H.U. and Bernt, E. (1974) 2-Oxoglutarate. In Methods of Enzymatic Analysis, 2nd edn., Vol. 3. Edited by Bergmeyer, H.U. pp. 1577-1580. Verlag Chemie, Weinheim.
    • (1974) Methods of Enzymatic Analysis, 2nd Edn. , vol.3 , pp. 1577-1580
    • Bergmeyer, H.U.1    Bernt, E.2
  • 5
    • 0015189585 scopus 로고
    • Control of leghaemoglobin synthesis in snake beans
    • Broughton, W.J. and Dilworth, M.J. (1971) Control of leghaemoglobin synthesis in snake beans. Biochem. J. 125: 1075-1080.
    • (1971) Biochem. J. , vol.125 , pp. 1075-1080
    • Broughton, W.J.1    Dilworth, M.J.2
  • 6
    • 0000756509 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: A ubiquitous, highly regulated enzyme in plants
    • Chollet, R., Vidal, J. and O'Leary, M.H. (1996) Phosphoenolpyruvate carboxylase: a ubiquitous, highly regulated enzyme in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47: 273-298.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 273-298
    • Chollet, R.1    Vidal, J.2    O'Leary, M.H.3
  • 7
    • 0000377892 scopus 로고
    • Carbon metabolism and compartmentation in nitrogen-fixing legume nodules
    • Day, D.A. and Copeland, L. (1991) Carbon metabolism and compartmentation in nitrogen-fixing legume nodules. Plant Physiol. Biochem. 29: 185-201.
    • (1991) Plant Physiol. Biochem. , vol.29 , pp. 185-201
    • Day, D.A.1    Copeland, L.2
  • 8
    • 0000013989 scopus 로고
    • Metabolite exchange across symbiosome membranes
    • Day, D.A. and Udvardi, M.K. (1992) Metabolite exchange across symbiosome membranes. Symbiosis 14: 175-189.
    • (1992) Symbiosis , vol.14 , pp. 175-189
    • Day, D.A.1    Udvardi, M.K.2
  • 9
    • 84989751801 scopus 로고
    • Nodule phosphoenolpyruvate carboxylase: A review
    • Deroche, M.E. and Carrayol, E. (1988) Nodule phosphoenolpyruvate carboxylase: a review. Physiol. Plant. 74: 775-782.
    • (1988) Physiol. Plant. , vol.74 , pp. 775-782
    • Deroche, M.E.1    Carrayol, E.2
  • 10
    • 0034928181 scopus 로고    scopus 로고
    • Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosphoenolpyruvate carboxylase
    • Dong, L., Ermolova, N.V. and Chollet, R. (2001) Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosphoenolpyruvate carboxylase. Planta 213: 379-389.
    • (2001) Planta , vol.213 , pp. 379-389
    • Dong, L.1    Ermolova, N.V.2    Chollet, R.3
  • 11
    • 0032703957 scopus 로고    scopus 로고
    • Expression of C-assimilating enzymes in pea (Pisum sativum L.) root nodules. In situ localization in effective nodules
    • Fedorova, M., Tikhonovich, I.A. and Vance, C.P. (1999) Expression of C-assimilating enzymes in pea (Pisum sativum L.) root nodules. In situ localization in effective nodules. Plant Cell Environ. 22: 1249-1262.
    • (1999) Plant Cell Environ. , vol.22 , pp. 1249-1262
    • Fedorova, M.1    Tikhonovich, I.A.2    Vance, C.P.3
  • 12
    • 0015181329 scopus 로고
    • Inactivation in vivo of glutamine synthetase and NAD-specific glutamate dehydrogenase: Its role in the regulation of glutamine synthesis in yeast
    • Ferguson, A.R. and Sims, S.P. (1971) Inactivation in vivo of glutamine synthetase and NAD-specific glutamate dehydrogenase: its role in the regulation of glutamine synthesis in yeast. J. Gen. Microbiol. 69: 423-427.
    • (1971) J. Gen. Microbiol. , vol.69 , pp. 423-427
    • Ferguson, A.R.1    Sims, S.P.2
  • 14
    • 0007411311 scopus 로고
    • Lotus jaopnicus, an autogamous, diploid legume species for classical and molecular genetics
    • Handberg, K. and Stougaard, J. (1992) Lotus jaopnicus, an autogamous, diploid legume species for classical and molecular genetics. Plant J. 2: 487-496.
    • (1992) Plant J. , vol.2 , pp. 487-496
    • Handberg, K.1    Stougaard, J.2
  • 15
    • 0001149734 scopus 로고
    • C4 photosynthesis: An unlikely process full of surprises
    • Hatch, M.D. (1992) C4 photosynthesis: an unlikely process full of surprises. Plant Cell Physiol. 33: 333-342.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 333-342
    • Hatch, M.D.1
  • 17
    • 0029664783 scopus 로고    scopus 로고
    • Evolution and expression of C4 photosynthesis genes
    • Ku, M.S., Kano-Murakami, Y. and Matsuoka, M. (1996) Evolution and expression of C4 photosynthesis genes. Plant Physiol. 111: 949-957.
    • (1996) Plant Physiol. , vol.111 , pp. 949-957
    • Ku, M.S.1    Kano-Murakami, Y.2    Matsuoka, M.3
  • 18
    • 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
  • 19
    • 84981653327 scopus 로고
    • Nitrogen fixation in the root nodules of Vicia faba L. in relation to the assimilation of carbon. II. the dark fixation of carbon dioxide
    • Lawrie, A.C. and Wheeler, C.T. (1975) Nitrogen fixation in the root nodules of Vicia faba L. in relation to the assimilation of carbon. II. The dark fixation of carbon dioxide. New Physiol. 74: 437-445.
    • (1975) New Physiol. , vol.74 , pp. 437-445
    • Lawrie, A.C.1    Wheeler, C.T.2
  • 20
    • 0000769546 scopus 로고
    • Sucrose synthase of soybean nodules
    • Morell, M. and Copeland, L. (1985) Sucrose synthase of soybean nodules. Plant Physiol. 78: 149-154.
    • (1985) Plant Physiol. , vol.78 , pp. 149-154
    • Morell, M.1    Copeland, L.2
  • 21
    • 0037383850 scopus 로고    scopus 로고
    • Characterization and expression analysis of genes encoding phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxylase kinase of Lotus japonicus, a model legume
    • Nakagawa, T., Izumi, T., Banba, M., Umehara, Y., Kouchi, H., Izui, K. and Hata, S. (2003) Characterization and expression analysis of genes encoding phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxylase kinase of Lotus japonicus, a model legume. Mol. Plant-Microbe Interact. 16: 281-288.
    • (2003) Mol. Plant-Microbe Interact. , vol.16 , pp. 281-288
    • Nakagawa, T.1    Izumi, T.2    Banba, M.3    Umehara, Y.4    Kouchi, H.5    Izui, K.6    Hata, S.7
  • 22
    • 0034142131 scopus 로고    scopus 로고
    • The regulation of phosphoenolpyruvate carboxylase in CAM plants
    • Nimmo, H.G. (2000) The regulation of phosphoenolpyruvate carboxylase in CAM plants. Trends Plant Sci. 5: 75-80.
    • (2000) Trends Plant Sci. , vol.5 , pp. 75-80
    • Nimmo, H.G.1
  • 23
    • 0034931337 scopus 로고    scopus 로고
    • Partial purification and characterization of a protein inhibitor of phosphoenolpyruvate carboxylase kinase
    • Nimmo, G.A., Wilkins, M.B. and Nimmo, H.G. (2001) Partial purification and characterization of a protein inhibitor of phosphoenolpyruvate carboxylase kinase Planta 213: 250-257.
    • (2001) Planta , vol.213 , pp. 250-257
    • Nimmo, G.A.1    Wilkins, M.B.2    Nimmo, H.G.3
  • 24
    • 20444375858 scopus 로고    scopus 로고
    • The promoter for C4-type mitochondrial aspartate aminotransferase does not direct bundle sheath-specific expression in transgenic rice plants
    • Nomura, M., Higuchi, T., Katayama, K., Taniguchi, M., Miyao-Tokutomi, M., Matsuoka, M. and Tajima, S. (2005) The promoter for C4-type mitochondrial aspartate aminotransferase does not direct bundle sheath-specific expression in transgenic rice plants. Plant Cell Physiol. 46: 743-753.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 743-753
    • Nomura, M.1    Higuchi, T.2    Katayama, K.3    Taniguchi, M.4    Miyao-Tokutomi, M.5    Matsuoka, M.6    Tajima, S.7
  • 25
    • 0020396945 scopus 로고
    • Phosphoenol-3-bromopyruvate. A mechanism-based inhibitor of phosphoenolpyruvate carboxylase from maize
    • O'Leary, M.H. and Diaz, E. (1982). Phosphoenol-3-bromopyruvate. A mechanism-based inhibitor of phosphoenolpyruvate carboxylase from maize. J. Biol. Chem. 257: 14603-14605.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14603-14605
    • O'Leary, M.H.1    Diaz, E.2
  • 28
    • 0000314267 scopus 로고
    • Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase
    • Schuller, K.A., Turpin, D.H. and Plaxton, W.C. (1990) Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase. Plant Physiol. 94: 1429-1435.
    • (1990) Plant Physiol. , vol.94 , pp. 1429-1435
    • Schuller, K.A.1    Turpin, D.H.2    Plaxton, W.C.3
  • 29
    • 0001692673 scopus 로고
    • Phosphorylation of soybean (Glycine max L.) nodule phosphoenolpyruvate carboxylase in vitro decreases sensitivity to inhibition by L-malate
    • Schuller, K.A. and Werner, D. (1993) Phosphorylation of soybean (Glycine max L.) nodule phosphoenolpyruvate carboxylase in vitro decreases sensitivity to inhibition by L-malate. Plant Physiol. 101: 1267-1273.
    • (1993) Plant Physiol. , vol.101 , pp. 1267-1273
    • Schuller, K.A.1    Werner, D.2
  • 30
    • 0032575877 scopus 로고    scopus 로고
    • Inhibition of alfalfa root nodule phosphoenolpyruvate carboxylase through an antisense strategy impacts nitrogen fixation and plant growth
    • Schulze, J., Shi, L., Blumenthal, J., Samac, D.A., Gantt, J.S. and Vance, C.P. (1998) Inhibition of alfalfa root nodule phosphoenolpyruvate carboxylase through an antisense strategy impacts nitrogen fixation and plant growth. Photochemistry 49: 341-346.
    • (1998) Photochemistry , vol.49 , pp. 341-346
    • Schulze, J.1    Shi, L.2    Blumenthal, J.3    Samac, D.A.4    Gantt, J.S.5    Vance, C.P.6
  • 31
    • 77956846102 scopus 로고
    • Transport and metabolism of carbon and nitrogen in legume nodules
    • Streeter, J.G. (1991) Transport and metabolism of carbon and nitrogen in legume nodules. Adv. Bot. Res. 18: 129-187.
    • (1991) Adv. Bot. Res. , vol.18 , pp. 129-187
    • Streeter, J.G.1
  • 32
    • 0031791902 scopus 로고    scopus 로고
    • Bacteroids isolated from infective nodules of Pisum sativum mutant E135 (sym13) lack nitrogenase activity but contain the two protein components of nitrogenase
    • Suganuma, N., Sonoda, N., Nakane, C., Hayashi, K., Hayashi, T., Tamaoki, M. and Kouchi, H. (1998) Bacteroids isolated from infective nodules of Pisum sativum mutant E135 (sym13) lack nitrogenase activity but contain the two protein components of nitrogenase. Plant Cell Physiol. 39: 1093-1098.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 1093-1098
    • Suganuma, N.1    Sonoda, N.2    Nakane, C.3    Hayashi, K.4    Hayashi, T.5    Tamaoki, M.6    Kouchi, H.7
  • 33
    • 0022709996 scopus 로고
    • Separation of amino acid and amide nitrogen from plant extracts for 15N analysis
    • Ta, T.C. and Joy, K. (1986) Separation of amino acid and amide nitrogen from plant extracts for 15N analysis. Anal. Biochem. 154: 564-569.
    • (1986) Anal. Biochem. , vol.154 , pp. 564-569
    • Ta, T.C.1    Joy, K.2
  • 34
    • 0345038520 scopus 로고
    • Metabolism of nitrogen fixed by nodules of alfalfa (Medicago sativa L.) H. Asparagine synthesis
    • Ta, T.C., Macdowall, F.D.H. and Faris, M.A. (1988) Metabolism of nitrogen fixed by nodules of alfalfa (Medicago sativa L.) H. Asparagine synthesis. Biochem. Cell Biol. 66: 1349-1354.
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 1349-1354
    • Ta, T.C.1    Macdowall, F.D.H.2    Faris, M.A.3
  • 35
    • 0008906332 scopus 로고
    • Succinate degradation through the citric acid cycle in Bradyrhizobium japonicum J501 bacteroids under low oxygen concentration
    • Tajima, S., Kimura, I., Kouzai, K. and Kasai, T. (1990) Succinate degradation through the citric acid cycle in Bradyrhizobium japonicum J501 bacteroids under low oxygen concentration. Agric. Biol. Chem. 54: 891-897.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 891-897
    • Tajima, S.1    Kimura, I.2    Kouzai, K.3    Kasai, T.4
  • 36
    • 2442675638 scopus 로고    scopus 로고
    • Ureide biosynthesis in legume nodules
    • Tajima, S., Nomura, M. and Kouchi, H. (2004) Ureide biosynthesis in legume nodules, Front. Biosci. 9: 1374-1381
    • (2004) Front. Biosci. , vol.9 , pp. 1374-1381
    • Tajima, S.1    Nomura, M.2    Kouchi, H.3
  • 37
    • 0032007276 scopus 로고    scopus 로고
    • Glutamate synthase and nitrogen assimilation
    • Temple, S.T., Vance, C.P. and Gantt, J.S. (1998) Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 3: 51-56.
    • (1998) Trends Plant Sci. , vol.3 , pp. 51-56
    • Temple, S.T.1    Vance, C.P.2    Gantt, J.S.3
  • 38
    • 0000427765 scopus 로고
    • Crassulacean acid metabolism
    • Ting, I.P. (1985) Crassulacean acid metabolism. Annu. Rev. Plant Physiol. 36: 595-622.
    • (1985) Annu. Rev. Plant Physiol. , vol.36 , pp. 595-622
    • Ting, I.P.1
  • 39
    • 0033993609 scopus 로고    scopus 로고
    • Immunological analysis of the phosphorylation state of maize C4-form phosphoenolpyruvate carboxylase with specific antibodies raised against a synthetic phosphorylated peptide
    • Ueno, Y., Imanari, E., Emura, J., Yoshizawa-Kumagaye, K., Nakajima, K., Inami, K., Shiba, T., Sakakibara, H., Sugiyama, T. and Izui, K. (2000) Immunological analysis of the phosphorylation state of maize C4-form phosphoenolpyruvate carboxylase with specific antibodies raised against a synthetic phosphorylated peptide. Plant J. 21: 17-26.
    • (2000) Plant J. , vol.21 , pp. 17-26
    • Ueno, Y.1    Imanari, E.2    Emura, J.3    Yoshizawa-Kumagaye, K.4    Nakajima, K.5    Inami, K.6    Shiba, T.7    Sakakibara, H.8    Sugiyama, T.9    Izui, K.10
  • 40
    • 0002762093 scopus 로고
    • Primary assimilation of nitrogen in alfalfa nodules: Molecular features of enzymes involved
    • Vance, C.P., Gergerson, R.G., Robinson, D.L., Miller, S.S. and Gantt, J.S. (1994) Primary assimilation of nitrogen in alfalfa nodules: molecular features of enzymes involved. Plant Sci. 101: 51-64.
    • (1994) Plant Sci. , vol.101 , pp. 51-64
    • Vance, C.P.1    Gergerson, R.G.2    Robinson, D.L.3    Miller, S.S.4    Gantt, J.S.5
  • 41
    • 0030925049 scopus 로고    scopus 로고
    • Regulatory phosphorylation of C4 PEP carboxylase
    • Vidal, J. and Chollet, R. (1997) Regulatory phosphorylation of C4 PEP carboxylase. Trends Plant Sci. 2: 230-237.
    • (1997) Trends Plant Sci. , vol.2 , pp. 230-237
    • Vidal, J.1    Chollet, R.2
  • 42
    • 0000477986 scopus 로고
    • Physiology of nitrogen-fixing legume nodules: Compartments and functions
    • Edited by Stacey, G., Burris, R.H. and Evans, H.J. Chapman and Hill, New York
    • Werner, D. (1992) Physiology of nitrogen-fixing legume nodules: compartments and functions. In Biological Nitrogen Fixation. Edited by Stacey, G., Burris, R.H. and Evans, H.J. pp. 399-431. Chapman and Hill, New York.
    • (1992) Biological Nitrogen Fixation , pp. 399-431
    • Werner, D.1
  • 43
    • 0028873231 scopus 로고
    • In vivo regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase
    • Zhang, X.Q., Li, B. and Chollet, R. (1995) In vivo regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase. Plant Physiol. 108: 1561-1568.
    • (1995) Plant Physiol. , vol.108 , pp. 1561-1568
    • Zhang, X.Q.1    Li, B.2    Chollet, R.3
  • 44
    • 0031571143 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: Partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots
    • Zhang, X.Q. and Chollet, R. (1997) Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots. Arch. Biochem. Biophys. 343: 260-268.
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 260-268
    • Zhang, X.Q.1    Chollet, R.2


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