Molecular and General Genetics MGG

, Volume 192, Issue 1–2, pp 110–117

Parallel induction and synthesis of PDC and ADH in anoxic maize roots

  • Andrei Laszlo
  • Patricia St. Lawrence
Article

Summary

The activity of pyruvate decarboxylase, PDC (EC 4.1.1.17), in the primary roots of maize seedlings exposed to anoxic conditions was examined: such treatment resulted in a time-dependent increase of enzymatic activity. We identified the polypeptide associated with PDC activity by two dimensional gel electrophoresis of electrophoretic mobility variants. The incorporation of radioactive amino acids into this polypeptide under anoxic conditions indicated that the increase in enzymatic activity was accompanied by the de novo synthesis of the PDC polypeptide and therefore identified PDC as one of the anaerobic proteins of maize. The increase in PDC activity paralleled that of alcohol dehydrogenase, ADH. Since PDC and ADH catalyze sequential reactions of the Embden-Meyerhoff pathway, our results define a system of apparent coordinate regulation of the expression of two metabolically related enzymatic activities in maize.

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References

  1. Berlin CM, Schimke RT (1965) Influence of turnover rates on the responses of enzymes to cortisone. Mol Pharmacol 1:149–156Google Scholar
  2. Bonner WM, Laskey RA (1974) A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem 46:83–88Google Scholar
  3. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of dye binding. Anal Biochem 72:248–254Google Scholar
  4. Cooke RJ, Grego S, Oliver J, Davies DD (1979) The effect of deuterium oxide on protein turnover in Lemna minor. Planta 146:229–236Google Scholar
  5. Cooke RJ, Grego S, Roberts K, Davies DD (1980) The mechanism of deuterium oxide induced protein degradation in Lemna minor. Planta 148:374–381Google Scholar
  6. Davies DD, Corbett RJ (1969) Glyoxylate decarboxylase activity in higher plants. Phytochemistry 8:529–542Google Scholar
  7. Davies DD, Davies S (1972) Purification and properties of l(+) lactate dehydrogenase from potato tubers. Biochem J 129:831–839Google Scholar
  8. Davies DD, Grego S, Kenworthy P (1974) The control of production of lactate and ethanol by higher plants. Planta 118:297–310Google Scholar
  9. Davis BJ (1964) Disc electrophoresis-II: Method and application to human serum proteins. Ann NY Acad Sci 121:404–427Google Scholar
  10. Ferl RJ, Dloughy SR, Schwartz D (1979) Analysis of maize alcohol dehydrogenase by native-SDS two dimensional electrophoresis and autoradiography. Mol Gen Genet 169:7–12Google Scholar
  11. Freeling M (1973) Simultaneous induction by anaerobiosis or 2–4 D of multiple enzymes specified by unlinked genes: differential ADH-1/ADH-2 expression in maize. Mol Gen Genet 127:215–227Google Scholar
  12. Hageman RH, Flescher D (1960) The effect of anaerobic environment on the activity of alcohol dehydrogenase and other enzymes in corn seedlings. Arch Biochem Biophys 87:203–208Google Scholar
  13. Holzer H, Schultz G, Villar-Palasi C, Juntgen-Sell J (1956) Isolierung der Hefecarboxylase und Untersuchungen über die Aktivität des Enzyms in lebenden Zellen. Biochem Z 327:331–337Google Scholar
  14. John CD, Greenway H (1976) Alcoholic fermentation and activity of some enzymes in rice roots. Aust J Plant Physiol 3:325–336Google Scholar
  15. Jornvall H, Fairwell T, Kratofil P, Wills C (1980) Differences in α-amino acetylation of isozymes of yeast alcohol dehydrogenase. FEBS Lett 111:214–218Google Scholar
  16. Laszlo A (1981) Maize pyruvate decarboxylase: an inducible enzyme. PhD Thesis, University of California, BerkeleyGoogle Scholar
  17. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685Google Scholar
  18. Leblova S, Zima J, Perglerova E (1976) Conversion of pyruvate under natural and artificial anaerobiosis in maize. Aust J Plant Physiol 3:755–761Google Scholar
  19. McClure WR (1969) A kinetic analysis of coupled enzyme assays. Biochemistry 7:2782–2786Google Scholar
  20. Okimoto R, Sachs M, Porter E, Freeling M (1980) Patterns of polypeptide synthesis in various maize organs under anaerobiosis. Planta 150:89–94Google Scholar
  21. Rothe GM (1976) Inhibition of plant lactate dehydrogenase isoenzymes by benzoic acid and cinnamic acid derivatives. Z Pflanzenphysiol 79:384–391Google Scholar
  22. Sachs M, Freeling M (1978) Selective synthesis of alcohol dehydrogenase during anaerobic treatment of maize. Mol Gen Genet 161:111–115Google Scholar
  23. Sachs M, Freeling M, Okimoto R (1980) The anaerobic proteins of maize. Cell 20:761–767Google Scholar
  24. Schellenberger A (1967) Structure and mechanism of action of the active center of yeast pyruvate decarboxylase. Angew Chem Int Ed Engl 6:1024–1035Google Scholar
  25. Schwartz D, Endo T (1966) Alcohol dehydrogenase polymorphism in maize: single and compound loci. Genetics 53:709–715Google Scholar
  26. Shriner R, Fuson RC, Curtin DY (1964) The systematic identification of organic compounds, ed 5. John Wiley and Sons, New YorkGoogle Scholar
  27. Wignarajah K, Greenway H (1976) Effect of anaerobiosis on the activities of alcohol dehydrogenase and pyruvate decarboxylase in roots of Zea mays. New Phytol 77:575–589Google Scholar
  28. Williams DE, Reisfeld RA (1964) Disc electrophoresis in polyacrylamide gels: extensions to new conditions of pH and buffer. Ann NY Acad Sci 121:373–381Google Scholar

Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • Andrei Laszlo
    • 1
  • Patricia St. Lawrence
    • 1
  1. 1.Genetics DepartmentUniversity of CaliforniaBerkeleyUSA
  2. 2.Department of Radiation OncologyUniversity of CaliforniaSan Francisco

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