Abstract
We have studied the effect of glucose on different enzyme activities in callus cultures of N.plumbaginifolia. We provided evidence that the increase in glucose concentration represses the synthesis of GDH, AcPh and MDH whereas ADH and LDH are unaffected. When glucose repressed cultures were transferred to the low glucose concentration medium the activity of GDH and AcPh resumed to the level shown by non repressed cultures. Sucrose and fructose were as effective as glucose in repressing GDH activity. These results support the hypothesis of the existence of a catabolite dependent regulation of enzyme synthesis in higher plants.
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Benkel, B. F.,Hickey, D. A.: ADrosophila gene is subject to glucose repression. - Proc. nat. Acad. Sci. USA84:1337–1339,1987.
Bernt, E., Bergmeyer, H. H.: Phosphatases. - In:Bergmeyer, H. H. (ed.): Methods of Enzymatic Analysis. Pp. 783–789. Academic Press, London 1963.
Duke, S. H, Koukkari, W. L.: Glutamate dehydrogenase activity inLemna perpusilla 6746: the effects of sucrose, glucose and fructose addition to growth media. - Physiol. Plant.39: 67–72,1977.
Gancedo, J. M., Gancedo, C.: Catabolite repression mutants of yeast. - FEMS Microbiol. Rev.32: 179–187,1986.
Handa, A. K., Bressan, R. A., Quader, H., Filner, P.: Association of formation and release of cyclic AMP with glucose depletion and onset of chlorophyll synthesis inPoterioochromonas malhamensis.- Plant Physiol.68: 460–463,1981.
Hanson, A. D., Jacobsen, J. V.: Control of lactate dehydrogenase, lactate glycolysis, and α-amylase by O2 deficit in barley aleurone layers. - Plant Physiol.75: 566–572,1984.
Joy, K. W.: Nitrogen metabolism inLemna minor. II. Enzymes of nitrate assimilation and some aspects of their regulation. -Plant Physiol.44: 849–853,1969.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. - J. biol. Clem.193: 265–275,1951.
Magasanik, B.: Catabolite repression. - Cold Spring Harb. Symp. Quant. Biol.26: 249–257,1961.
Polakis, E. S., Bartley, W.: Changes in the enzyme activities ofSaccharomyces cerevisiae during aerobic growth on different carbon sources. - Biochem J.97: 284–297,1965.
Prunkard, D. E., Bascomb, N. F., Molin, W. T., Schmidt, R. R.: Effect of different carbon sources on the ammonium induction of different forms of NADP-specific glutamate dehydrogenase inChlorella sorokiniana cells cultured in the light and dark. - Plant Physiol.81: 413–422,1986.
Queiroz, O.: Photoperiodisme et activité enzymatique (PEP carboxylase et enzyme malique) dans les feuillesdeKalanchoe blossfeldiana.- Phytochemistry8: 1655–1663, 1969.
Restivo, F. M., Tassi, F., Maestri, E., Lorenzoni, C., Puglisi, P. P., Marmiroli, N.: Identification of chloroplast associated heat-shock proteins inNicotiana plumbaginifolia protoplasts. -Curr. Genet.11:145–149,1986.
Sahulka, J., Lisá, L.: Effect of some disaccharides, hexoses and pentoses on nitrate reductase, glutamine synthetase and glutamate dehydrogenase in excised pea roots. - Physiol. Plant.50: 32–36,1980.
Snell, F. D., Snell, C. T.: Colorimetric Method of Analysis. Vol. III. Pp. 204–207. D. Van Nostrand Comp. Inc., Wokingham 1953.
Tassi, F., Restivo, F. M., Ferrari, G., Puglisi, P. P.: Erythromycin as a tool for discriminating in vivo between mitochondrial and chloroplastic protein synthesis inNicotiana sylvestris. - Plant Sci. Lett.29: 215–225,1983.
Tassi, F., Restivo, F. M., Puglisi, P. P., Cacco, G.: Effect of glucose on glutamate dehydrogenase and add phosphatase and its reversal by cyclic adenosine 3': 5'-monophosphate in single cell cultures ofAsparagus officinalis. - Physiol. Plant.60 : 61–64,1984.
Ullmann, A.: Catabolite repression 1985. - Biochimie67: 29–34,1985.
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Restivo, F.M., Tassi, F., Maestri, E. et al. The ’glucose effect’ in callus cultures ofNicotiana plmmbaginifolia is enzyme specific. Biol Plant 31, 104–112 (1989). https://doi.org/10.1007/BF02907240
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DOI: https://doi.org/10.1007/BF02907240