Planta

, Volume 151, Issue 2, pp 168–175 | Cite as

Evolution of carboxylating enzymes involved in paramylon synthesis (phosphoenolpyruvate carboxylase and carboxykinase) in heterotrophically grown Euglena gracilis

  • Joël Briand
  • Régis Calvayrac
  • Danielle Laval-Martin
  • Jack Farineau
Article

Abstract

Heterotrophically grown Euglena synthesize grains of paramylon, its reserve carbohydrate, in a vesicular complex of mitochondrial origin. A CO2 fixation activity in dark grown Euglena was demonstrated in the mitochondria via paramylon. At the beginning of the exponential phase of growth, the activity of phosphoenolpyruvate carboxykinase increases before the augmentation of paramylon.

At the end of the exponential phase, the activity of this enzyme decreases, and low residual levels persist in the transition and stationary phases of growth. The activity of phosphoenolpyruvate carboxylase evolves inversely during the heterotrophic growth of the algae in succinate- or a lactate-containing medium. A compartmentalized scheme of carbon metabolism in mitochondria is presented.

Key words

Carbon metabolism Euglena Mitochondria Paramylon Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase 

Abbreviations

PEP

phosphoenolpyruvate

OAA

oxaloacetate

PGA

phosphoglyceric acid

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References

  1. Barras, D.R., Stone, B.A. (1968) Carbohydrate composition and metabolism in Euglena. In: Biology of Euglena, pp. 149–191 Buetow E., ed., Academic Press. New York and LondonGoogle Scholar
  2. Bray, G.A. (1960) A simple effluent liquid scintillation method for counting aqueous solutions in a liquid scintillation counter. Anal. Biochem. 1, 279–285Google Scholar
  3. Briand, J., Calvayrac, R. (1980) Paramylon synthesis in heterotrophic and photoheterotrophic Euglena. J. Phycol. 16, 234–239Google Scholar
  4. Calvayrac, R. (1970) Relation entre les subtrats, la respiration et la structure mitochondriale chez Euglena gracilis Z. Arch. Mikrobiol. 73, 308–314Google Scholar
  5. Calvayrac, R. (1972) Le cycle des mitochondries chez Euglena gracilis en culture synchrone. Thèse de Doctorat, Univ. Paris XIGoogle Scholar
  6. Calvayrac, R., Ledoigt, G. (1976) Croissance des Euglènes en présence de DCMU: Evolution du plastidome en fonction de la tension d'oxygène. Plant Sci. Lett. 7, 249–263Google Scholar
  7. Calvayrac, R., Levy, M., Vazart, J., Briand, J., Claisse, M. (1978) Activité cytochrome oxydase des mitochondries d'Euglena gracilis Z: Comparaison de l'action du ferrocytochrome c 558 et due ferrocytochrome c de mammifères. Biol. Cell, 31, 141–148Google Scholar
  8. Calvayrac, R., Briand, J. (1978) Paramylon synthesis and the chondriome of Euglena gracilis Z. In: Plant mitochondria, pp. 435–443 G. Ducet and C. Lance, eds. Elsevier North HollandGoogle Scholar
  9. Calvayrac, R., Bomsel, J.L., Laval-Martin, D. (1979) Analysis and characterization of DCMU resistant Euglena. I. Growth, metabolic and ultrastructural modifications during adaptation to different doses of DCMU. Plant Physiol. 63, 857–865Google Scholar
  10. Codd, G.A., Merrett, M.J. (1971) Phosphopyruvate carboxylase activity and carbon dioxide fixation via C4 acids over the division cycle in synchronized Euglena cultures. Planta 100, 124–130Google Scholar
  11. Colman, B., Cheng, K.H., Ingle, R.K. (1976) The relative activities of phosphoenol-pyruvate carboxylase and ribulose di-phosphate carboylase in blue-green algae. Plant Sci. Lett. 6, 123–127Google Scholar
  12. Cook, J.R. (1965) Influence of light on acetate utilization in green Euglena. Plant Cell Physiol. 6, 301–307Google Scholar
  13. Conn, E.E., Stumpf, P.K. (1976) Outlines of Biochemistry (1976) John Wiley and sons Pub. pp. 294Google Scholar
  14. Cramer, M.L., Myers, J. (1952) Growth and photosynthetic characteristics of Euglena gracilis. Arch. Mikrobiol. 17, 384–402Google Scholar
  15. Dittrich, P., Campbell, W.H., Black, C.C. (1973) Phosphoenol pyruvate carboxykinase in plants exhibiting Crassulacean acid metabolism. Plant Physiol. 52, 357–361Google Scholar
  16. Drobnica, L., Ebringer, L. (1962) The determination of the activity of some enzymes of carbon metabolism in extracts of Euglena gracilis cells. Folia Microbiol. (Prague) 8, 56–59Google Scholar
  17. Edwards, G.E., Kanai, R., Black, C.C. (1971) Phosphoenol pyruvate carboxykinase in leaves of certain plants with fix CO2 by the C4 dicarboxylic acid cycle of photosynthesis. Biochem. Biophys. Res. Comm. 45, 278–285PubMedGoogle Scholar
  18. Jomain-Baum, M., Schramm, V.L., Hanson, R.W. (1976) Mechanism of 3-mercaptopicolinic acid inhibition of hepatic phosphoenolpyruvate carboxykinase (GTP) J. Biol. Chem. 251, 37–44PubMedGoogle Scholar
  19. Karn, R.C., Kivic, P.A., Hudock, G.A. (1973) A procedure for the electrophoretic analysis of PEPcase. Biochim. Biophys. Acta 293, 567–569PubMedGoogle Scholar
  20. Laval-Martin, D., Farineau, J., Diamond, J. (1977) Light versus dark carbon metabolism in cherry Tomato fruits. I occurence of photosynthesis. Study of the intermediates. Plant Physiol. 60, 872–876Google Scholar
  21. Leegood, R.C., Rees, T. (1978) Dark fixation of CO2 during gluconeogenesis by the cotyledons of Cucurbita pepo L. Planta 140, 275–282Google Scholar
  22. Leveldahl, B.H. (1966) Heterotrophic CO2 fixation by a bleached Euglena. Exp. Cell Res 44, 393–402PubMedGoogle Scholar
  23. Levedahl, B.H. (1967) The effect of CO2 on succinate metabolism in a bleached Euglena. Exp. Cell Res. 48, 125–131PubMedGoogle Scholar
  24. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265–275PubMedGoogle Scholar
  25. Lynch, V.H., Calvin, M. (1953) CO2 fixation by Euglena Ann. N.Y. Acad. Sci., 56, 890PubMedGoogle Scholar
  26. Mazelis, M., Vennesland, B. (1957) Carbon dioxide fixation into oxalacetate in higher plants. Plant Physiol. 32, 591–600Google Scholar
  27. Morot-Gaudry, J.F., Farineau, J. (1978) Etude comparée des réactions de carboxylations photosynthétiques chez un Maïs normal (W 64 A) et chez un Maïs mutant opaque 2 (W 64 A o 2): mise en évidence de déviations métaboliques chez le mutant. Physiol. Vég. 16, 451–467Google Scholar
  28. Ohmann, E., Plhâk, F. (1969) Reinigung und Eigenschaften von Phosphoenolpyruvat-case aus Euglena gracilis. Eur. J. Biochem. 10, 43–55PubMedGoogle Scholar
  29. Perl, M. (1974) Phosphoenolpyruvate carboxylating enzyme in dark-grown and in green Euglena cells. J. Biochem. 76, 1095–1101PubMedGoogle Scholar
  30. Wolpert, J.S., Ernst-Fonberg, M.L. (1975) A multi enzymes complex for CO2 fixation. Biochemistry 14, 1095–1102PubMedGoogle Scholar
  31. Wolpert, J.S., Ernst-Fonberg, M.L. (1975) Dissociation and characterization of enzymes from a multi-enzymes complex involved in CO2 fixation. Biochemistry 14, 1103–1107PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • Joël Briand
    • 1
  • Régis Calvayrac
    • 1
  • Danielle Laval-Martin
    • 1
  • Jack Farineau
    • 2
  1. 1.Laboratoire des Membranes BiologiquesUniversité Paris VIIParis Cedex 05France
  2. 2.Service de Biophysique de Département de BiologieComissariat à l'Energie AtomiqueGif-sur-YvetteFrance

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