Abstract
The phosphorylation state and the malate sensitivity of phosphoenolpyruvate carboxylase (PEPCase, EC 4.1.1.31) in Bryophyllum fedtschenkoi Hamet et Perrier are altered by changes in the ambient temperature. These effects, in turn alter the in-vivo activity of the enzyme. Low temperature (3 °C or less), stabilizes the phosphorylated form of the enzyme, while high temperature (30 °C) promotes its dephosphorylation. The catalytic activity of the phosphorylated and dephosphorylated forms of PEPCase increases with temperature, but the apparent K i values for malate of both forms of the enzyme decrease. Results of experiments with detached leaves maintained in darkness in normal air indicate that the changes in malate sensitivity and phosphorylation state of PEPCase with temperature are of physiological significance. When the phosphorylated form of PEPCase is stabilized by reducing the temperature of leaves 9 h after transfer to constant darkness at 15 °C, a prolonged period of CO2 fixation follows. When leaves are maintained in constant darkness at 15 °C until CO2 output reaches a low steady-state level and the PEPCase is dephosphorylated, reducing the temperature to 3 °C results in a further period of CO2 fixation even though the phosphorylation state of PEPCase does not change.
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Abbreviations
- CAM:
-
Crassulacean acid metabolism
- PEP:
-
phosphoenolpyruvate
- PEPCase:
-
phosphoenolpyruvate carboxylase
References
Anderson, C.M., Wilkins, M.B. (1989a) Period and phase control by temperature in the circadian rhythm of CO2 exchange in illuminated leaves of Bryophyllum fedtschenkoi. Planta 177, 456–469
Buchanan-Bollig, I.C., Kluge, M., Müller, D. (1984) Kinetic changes with temperature of phosphoenolpyruvate carboxylase from a CAM plant. Plant Cell Environ. 7, 63–70
Carter, P.J., Nimmo, H.G., Fewson, C.A., Wilkins, M.B. (1990) Bryophyllum fedtschenkoi protein phosphatase type 2A can dephosphorylate phosphoenolpyruvate carboxylase. FEBS Lett. 63, 233–236
Carter, P.J., Nimmo, H.G., Fewson, C.A., Wilkins, M.B. (1991) Circadian rhythms in the activity of a plant protein kinase. EMBO J. 10, 2063–2068
Carter, P.J., Wilkins, M.B., Nimmo, H.G., Fewson, C.A. (1995) The role of temperature in the regulation of the circadian rhythm of CO2 fixation in Bryophyllum fedtschenkoi. Planta 196, 383–388
Cohen, P., Alemany, S., Hemmings, B.A., Resink, T.J., Stralfors, P., Tung, L.H.Y. (1988) Protein phosphatase-1 and protein phosphatase-2 from rabbit skeletal muscle. Methods Enzymol. 159, 427–437
Friemert, V., Heininger, D., Kluge, M., Ziegler, H. (1988) Temperature effects on malic-acid efflux from the vacuoles and on the carboxylation pathways in Crassulacean-acid-metabolism plants. Planta 174, 453–461
Jones, R., Wilkins, M.B., Coggins, J.R., Fewson, C.A., Malcolm, A.D.B. (1978) Phosphoenolpyruvate carboxylase from the Crassulacean acid metabolism plant Bryophyllum fedtschenkoi Hamet et Perrier. Biochem. J. 175, 391–406
Kluge, M., Klienchen, A., Galla, H-J. (1991) Temperature effects on crassulacean acid metabolism: EPR spectroscopic studies on the thermotropic phase behaviour of the tonoplast membranes in Kalanchoë daigremontiana. Bot Acta 104, 355–360
McGowan, C.H., Cohen, P. (1988) Protein phosphatase-2C from rabbit skeletal muscle and liver. An Mg2+ dependent enzyme. Methods Enzymol. 159, 416–426
Nimmo, G.A., Nimmo, H.G., Fewson, C.A., Wilkins, M.B. (1984) Diurnal changes in the properties of phosphoenolpyruvate carboxylase in Bryophyllum leaves: a possible covalent modification. FEBS Lett. 178, 199–203
Nimmo, G.A., Nimmo, H.G., Hamilton, I.D., Fewson, C.A., Wilkins, M.B. (1986) Purification of the phosphorylated night form and dephosphorylated day form of phosphoenolpyruvate carboxylase from Bryophyllum fedtschenkoi. Biochem. J. 239, 213–220
Nimmo, G.A., Nimmo, H.G., Fewson, C.A., Wilkins, M.B. (1987) Persistent circadian rhythms in the phosphorylation state of phosphoenolpyruvte carboxylase from Bryophyllum fedtschenkoi leaves and in its sensitivity to inhibition by malate. Planta 170, 408–415
O'Leary, M.H. (1982) Phosphoenolpyruvate carboxylase: an enzymologist's view. Annu. Rev. Plant Physiol. 33, 297–315
Osmond, C.B. Holtum, J.A.M. (1981) Crassulacean acid metabolism. In: Plant Biochemistry, a comprehensive treatise, vol 8, pp. 283–328. Hatch, M.D., Boardman, N.K., eds. Academic Press, New York London
Pays, A.G.G., Jones, R., Wilkins, M.B., Fewson, C.A., Malcolm, A.D.B. (1980) Kinetic analysis of effectors of phosphoenolpyruvate carboxylase from Bryophyllum fedtschenkoi. Biochim. Biophys. Acta 614, 151–162
Wilkins, M.B. (1959) An endogenous rhythm in the rate of carbon dioxide ouput of Bryophyllum I. Some preliminary experiments. J. Exp. Bot. 10, 377–390
Wilkins, M.B. (1960) An endogenous rhythm in the rate of carbon dioxide output of Bryophyllum II. The effects of light and darkness on the phase and period of the rhythm. J. Exp. Bot. 11, 269–288
Wilkins, M.B. (1962) An endogenous rhythm in the rate of carbon dioxide output of Bryophyllum III. The effects of temperature on the phase and period of the rhythm. Proc. R. Soc. London 156, 220–241
Wilkins, M.B. (1973) An endogenous rhythm in the rate of carbon dioxide output of Bryophyllum. VI. Action spectrum for the induction of phase-shifts by visible radiation. J. Exp. Bot. 24, 488–496
Wilkins, M.B. (1983) The circadian rhythm of carbon-dioxide metabolism in Bryophyllum: the mechanism of phase-shift induction by thermal stimuli. Planta 157, 471–480
Wilkins, M.B. (1984) A rapid circadian rhythm of carbon-dioxide metabolism in Bryophyllum fedtschenkoi. Planta 161, 381–384
Wilkins, M.B. (1992) Circadian rhythms: their origin and control. New Phytol. 121, 347–375
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We thank the Agricultural and Food Research Council for financial support for this work.
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Carter, P.J., Wilkins, M.B., Nimmo, H.G. et al. Effects of temperature on the activity of phosphoenolpyruvate carboxylase and on the control of CO2 fixation in Bryophyllum fedtschenkoi . Planta 196, 375–380 (1995). https://doi.org/10.1007/BF00201398
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DOI: https://doi.org/10.1007/BF00201398