Abstract
The distribution of the two glutamate-synthase (GOGAT) activities known to exist in higher plants (NADH dependent, EC 2.6.1.53; and ferredoxin dependent, EC 1.4.7.1) was studied in non-chlorophyllous and chlorophyllous cultured tissue as well as in young leaves of Bouvardia ternifolia. The NADH-GOGAT was present in all three tissues. Using a sucrose gradient we found it in both the soluble and the plastid fraction of non-chlorophyllous and chlorophyllous tissue, but exclusively in the chloroplast fraction of the leaves. Ferredoxin-GOGAT was found only in green tissues and was confined to the chloroplasts. Ferredoxin-GOGAT activity increased in parallel with the chlorophyll content of the callus during the greening process in Murashige-Skoog medium (nitrate and ammonium as the nitrogen sources), while NADH-GOGAT was not affected by the greening process in this medium. Furthermore, both activities were differentially affected by either nitrate or ammonium as the sole nitrogen source in the medium during this process. It is suggested that each GOGAT activity is a different entity or is differently regulated.
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Abbreviations
- GOGAT:
-
glutamate synthase
- MS:
-
Murashige-Skoog (1962) medium
- PMSF:
-
phenylmethylsulfonyl fluoride
References
Arnon, D.I. (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1–15
Arima, Y. (1978) Glutamate synthase in rice extract and the relationship among electron donors, nitrogen donors and its activity. Plant Cell Physiol. 19, 955–961
Buchanan, B.B., Arnon, D.I. (1971) Ferredoxin from spinach leaves. Methods Enzymol. 23, 419–426
Dennis, D., Kaplan, N.O. (1962) Lactic acid racemase from Elostridium Butylicum. Methods Enzymol. 5, 430–431
Fernández, L., Sánchez de Jiménez, E. (1982) In vitro culture of Bouvardia ternifolia. Can. J. Bot. 60, 917–921
Gornall, A.G., Bardawill, Ch.J., David, M.M. (1949) Determination of serum proteins by means of the Biuret reaction. J. Biol. Chem. 177, 751–766
Losada, M., Paneque, A. (1971) Nitrite reductase, Methods Enzymol. 23, 487–492
Matoh, T., Takahashi, E. (1981) Glutamate synthase in greening pea shoots. Plant Cell Physiol. 22, 727–731
Matoh, T., Takahashi, E. (1982) Changes in the activity of ferredoxin and NADH glutamate synthase during seedling development of peas. Planta 154, 289–294
Miflin, B.J., Lea, P.J. (1980) Ammonium assimilation. In: The biochemistry of plants, vol. 5: Amino acids and derivative, pp. 169–180, Miflin, B.J., ed. Academic Press, New York London
Murashige, T., Skoog, T. (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Plant Physiol. 15, 473–497
Power, J.B., Cocking, E.C. (1970) Isolation of leaf protoplast. Macro-molecular uptake and growth substance response. J. Exp. Bot. 21, 64–70
Quail, P.H. (1979) Plant cell fractionation. Annu. Rev. Plant Physiol. 30, 425–484
Somerville, C.R., Ogren, W.L. (1980) Inhibition of photosynthesis in Arabidopsis mutants lacking leaf glutamate synthase activity. Nature 289, 257–259
Susuki, A., Vidal, J., Gadal, P. (1982) Glutamate synthase isoforms in rice. Plant Physiol. 70, 827–832
Wallsgrove, R.M., Lea, P.J., Miflin, B.J. (1979) The distribution of the enzymes of nitrogen assimilation within the pea leaf cell. Plant Physiol. 63, 232–236
Wallsgrove, R.M., Lea, P.J., Miflin, B.J. (1982) The development of NAD(P)H dependent and ferredoxin dependent glutamate synthase in greening barley and pea leaves. Planta 154, 473–476
Wharton, D.F., Tzagaloff, A. (1967) Cytochrome from beef hast mitochondria. Methods Enzymol. 10, 245–249
Woo, K.C., Morot-Gaudry, J.F., Summons, R.E., Osmond, C.B. (1982) Evidence for the glutamine synthetase/glutamate synthase pathway during the photorespiratory cycle in spinach leaves. Plant Physiol. 70, 1514–1517
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Murillo, E., Sánchez de Jiménez, E. Glutamate synthase in greening callus of Bouvardia ternifolia Schlecht. Planta 163, 448–452 (1985). https://doi.org/10.1007/BF00392701
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DOI: https://doi.org/10.1007/BF00392701