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Interaction of Chloroplast and Nuclear Genomes in Regulating RuBP Carboxylase Activity

  • S. D. Kung
  • P. R. Rhodes
Part of the Basic Life Sciences book series (BLSC, volume 11)

Abstract

Extensive studies of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase have provided much information on its structure, function, biosynthesis, mode of inheritance, and genetic variability (1-3). RuBP carboxylase, which in higher plants has been termed Fraction I protein, is found in all photosynthetic organisms as an oligomeric protein of high molecular weight (1-4). It catalyzes the carboxylation of RuBP, producing two molecules of glycerate 3-phosphate (PGA), the primary product of photosynthesis (3). In the presence of molecular oxygen, RuBP carboxylase can also catalyze the oxidation of RuBP, forming PGA and phosphoglycolate, which can be converted to glycolate, the substrate for photorespiration (3, 5). Since the balance between photosynthetic and photorespiratory processes determines a plant’s maximum yield, the ability of RuBP carboxylase to participate in either process has generated renewed interest in this enzyme.

Keywords

Large Subunit Small Subunit Chloroplast Genome Nuclear Genome Male Sterile Line 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Baker, T. S., Suh, S. W., and Eisenberg, D., Proc. Natl. Acad. Sei. USA 74, 1037–41 (1977).CrossRefGoogle Scholar
  2. 2.
    Kung, S. D., Science 191, 429–34 (1976).PubMedCrossRefGoogle Scholar
  3. 3.
    Jensen, R. G. and Bahr, J. T., Annu. Rev. Plant Physiol. 28, 379–400 (1977).CrossRefGoogle Scholar
  4. 4.
    Kawashima, N. and Wildman, S. G., Annu. Rev. Plant Physiol. 21, 325–58 (1970).CrossRefGoogle Scholar
  5. 5.
    Tolbert, N. E. and Ryan, F.J., in Proc. 3rd Int. Congr. Photosynthesis, pp. 1303–19, M. Avron, Editor, Elsevier, Amsterdam, (1974).Google Scholar
  6. 6.
    Hirai, A., Proc. Natl. Acad. Sei. USA 74, 3443–5 (1977).CrossRefGoogle Scholar
  7. 7.
    Nishimura, M. and Akazawa, T., Biochemistry 13, 2277–81 (1974).PubMedCrossRefGoogle Scholar
  8. 8.
    McFadden, B. A., Biochem. Biophys. Res. Commun. 60, 312–17 (1974).PubMedCrossRefGoogle Scholar
  9. 9.
    Paech, C. et al., See paper in this Symposium.Google Scholar
  10. 10.
    Chen, S., Johal, S., and Wildman, S.G., in Genetics and Biogenesis of Chloroplasts and Mitochondria, pp. 3–11, Th. Bucher et al., Editors, Elsevier, Amsterdam, 1976.Google Scholar
  11. 11.
    Kung, S. D., Sakano, K., and Wildman, S. G., Biochim. Biophys. Acta 365, 138–47 (1974).PubMedGoogle Scholar
  12. 12.
    Kung, S. D., Lee, C. I., Wood, D. D., and Moscarello, M. A., Plant Physiol. 60, 89–94 (1977).PubMedCrossRefGoogle Scholar
  13. 13.
    Chen, K., Kung, S. D., Gray, J. C., and Wildman, S. G., Plant Sei. Lett. 7, 429–34 (1976).CrossRefGoogle Scholar
  14. 14.
    Gray, J. Q., Kung, S. D., and Wildman, S. G., Arch. Biochem. Biophys. 185, 272–81 (1978).PubMedCrossRefGoogle Scholar
  15. 15.
    Sakano, K., Kung, S. D., and Wildman, S. G., Mol. Gen. Genet. 130, 91–7 (1974).CrossRefGoogle Scholar
  16. 16.
    Robinson, A. B. and Rudd, C. J., Curr. Top. Cell. Regul. 8, 247–95 (1974).PubMedGoogle Scholar
  17. 17.
    Williamson, A. R., Salaman, M. R., and Kreth, H. W., Ann. N.Y. Acad. Sei. 209, 210–16 (1973).CrossRefGoogle Scholar
  18. 18.
    Link, G. L. et al., See paper in this Symposium.Google Scholar
  19. 19.
    StrjJbaek, S., Gibbons, G. C, Haslett, B., and Wildman, S. G., Carlsberg Res. Commun 41, 335–9 (1976).CrossRefGoogle Scholar
  20. 20.
    Blair, G. E. and Ellis, R. J., Biochim. Biophys. Acta 319, 223–34 (1973).PubMedGoogle Scholar
  21. 21.
    Gray, J. C. and Kekwick, R. G. O., Eur. J. Biochem. 44, 491–500 (1974).PubMedCrossRefGoogle Scholar
  22. 22.
    Highfield, P. E. and Ellis, R. J., Nature London 271, 420–4 (1978)CrossRefGoogle Scholar
  23. 23.
    Chua, N. H. and Schmidt, G. W., See paper in this Symposium.Google Scholar
  24. 24.
    Kung, S. D., Annu. Rev. Plant Physiol. 28, 401–37 (1977).CrossRefGoogle Scholar
  25. 25.
    Gray, J. C., Kung, S. D., Wildman, S. G., and Sheen, S. J., Nature London 252, 226–7 (1974).PubMedCrossRefGoogle Scholar
  26. 26.
    Kung, S. D., Sakano, K., Gray, J. C., and Wildman, S. G., J. Mol. Evol. 7, 59–64 (1975).PubMedCrossRefGoogle Scholar
  27. 27.
    Sheen, S. J., Evolution 26, 143–54 (1972).CrossRefGoogle Scholar
  28. 28.
    Kung, S. D., Unpublished data.Google Scholar
  29. 29.
    Lee-Chang, C. I., Master’s thesis, U. of Maryland Baltimore County, Catonsville, 1977.Google Scholar
  30. 30.
    Chen, K., Ph.D. Thesis, U. of California, Los Angeles, 1974.Google Scholar
  31. 31.
    Rhodes, P. R. and Kung, S. D., In preparation.Google Scholar
  32. 32.
    Kung, S. D., Rhodes, P. R., Lee-Chang, C. I., Marsho, T. V., and Wood, D. D., Plant Physiol., submitted.Google Scholar
  33. 33.
    Kostoff, D., Cytogenetics of the Genus Nicotiana, p. 1071, State Printing House, Sofia, Bulgaria, 1943.Google Scholar
  34. 34.
    Burk, L. G., J. Hered. 64, 348–50 (1973).Google Scholar
  35. 35.
    Lorimer, G. H. and Badger, M. R., Anal. Biochem. 78, 66–73 (1977).PubMedCrossRefGoogle Scholar
  36. 36.
    Kung, S. D., Chollet, R., and Marsho, T. V., Methods Enzymol., in press (1978).Google Scholar
  37. 37.
    Kawashima, N., Tanabe, Y., and Iwai, S., Biochim. Biophys. Acta 427, 70–7 (1976).PubMedGoogle Scholar
  38. 38.
    Bogorad, L., Science 188, 891–8 (1975).PubMedCrossRefGoogle Scholar
  39. 39.
    Blamire, J., Flechtner, V. R., and Sager, R., Proc. Natl. Acad. Sei. USA 71, 2867–71 (1974).CrossRefGoogle Scholar
  40. 40.
    Mendiola-Morgenthaler, L. R., Morgenthaler, J. J., and Price, C. A., FEBS Lett. 62, 96–100 (1976).PubMedCrossRefGoogle Scholar
  41. 41.
    Klein, J. L. and Edwards, D. L., J. Biol. Chem. 250, 5852–6 (1975).PubMedGoogle Scholar
  42. 42.
    Lorimer, G. H. and Andrews, T. J., Nature London 243, 359–60 (1973).CrossRefGoogle Scholar
  43. 43.
    Steer, M. W. and Kernoghan, D., Biochem. Genet. 15, 273–86 (1977).PubMedCrossRefGoogle Scholar
  44. 44.
    Chen, K., Gray, J. C., and Wildman, S. G., Science 190, 1304–6 (1975).Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • S. D. Kung
    • 1
  • P. R. Rhodes
    • 1
  1. 1.Department of Biological SciencesUniversity of Maryland Baltimore CountyCatonsvilleUSA

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