Journal of Biosciences

, Volume 4, Issue 4, pp 431–439 | Cite as

Regulation of phosphoglycerate mutase in developing forespores and dormant spores ofBacillus megaterium by thein vivo levels of phosphoglycerate mutase inhibitor

  • Ravendra Pal Singh


Bacillus megaterium accumulated 3-phosphoglycerate during sporulation which was utilized during spore germination. During sporulation a protein was synthesized before or at the start of 3-phosphoglycerate accumulation inside the developing spores about 1.5 h before dipicolinic acid accumulation. This protein has an affinity for Mn2+ and other divalent metal ions and inhibits phosphoglycerate mutase activity which has been shown to require Mn2+ However, the levels of the inhibitor decreased considerably (75–85%) during spore germination. No appreciable amount of the inhibitor was detected in the vegetable cell and mother cell compartment; however, the forespore compartment possesses an activity comparable to that of dormant spores. The partially purified inhibitor has a molecular weight of 11,000 and possesses both high and low affinity binding sites for Mn2+ and Ca2+ as determined by Scatchard plot analysis.


Bacillus megaterium 3-phosphoglyceric acid phosphoglycerate mutase mutase inhibitor dipicolinic acid 

Abbreviations used


3-phosphoglyceric acid


2-phosphoglyceric acid


dipicolinic acid


supplemented nutrient broth


diethylamino ethyl


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  1. Czok, R. (1974)In Methods of enzymatic analysis (Academic Press Inc., New York), Vol. 3, p. 1414.Google Scholar
  2. Englund, P. T., Huberman, J. A., Jovin, T. M. and Kornberg, A. (1969)J. Biol Chem.,244, 3038.PubMedGoogle Scholar
  3. Gould, G. W. (1977)J. Appl Bacteriol.,42, 297.PubMedGoogle Scholar
  4. Gould, G. W. and Dring, G. J. (1975)Nature (London),258, 402.CrossRefGoogle Scholar
  5. Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951)J. Biol Chem.,193, 625.Google Scholar
  6. Nelson, D. L. and Kornberg, A. (1970)J. Biol Chem.,245, 1137.PubMedGoogle Scholar
  7. Oh, Y. K. and Freese, E. (1976)J. Bacteriol.,127, 739.PubMedGoogle Scholar
  8. Rotman, Y. and Field, M. I. (1967)Anal. Biochem.,22, 168.CrossRefGoogle Scholar
  9. Sacks, L. E. and Bailey, G. E. (1963)J. Bacteriol.,85, 720.PubMedGoogle Scholar
  10. Scatchard, G. (1949)Ann. New YorkAcad. Sci.,51, 660.CrossRefGoogle Scholar
  11. Setlow, P. and Kornberg, A. (1969)J. Bacteriol.,100, 1155.PubMedGoogle Scholar
  12. Setlow, P. and Kornberg, A. (1970a)J. Biol Chem.,245, 3637.PubMedGoogle Scholar
  13. Setlow, P. and Kornberg, A. (1970b)J. Biol Chem.,245, 3645.PubMedGoogle Scholar
  14. Setlow, B. and Mansour, T. E. (1972)Biochemistry,11, 1478.PubMedCrossRefGoogle Scholar
  15. Setlow, B. and Setlow, P. (1980)Proc. NatlAcad. Sci. (USA),77, 2474.CrossRefGoogle Scholar
  16. Singh, R. P. (1982)Indian J. Exp. Biol.,20, 223.Google Scholar
  17. Singh, R. P., Setlow, B. and Setlow, P. (1977)J. Bacteriol.,130, 1130.PubMedGoogle Scholar
  18. Singh, R. P., and Setlow, P. (1978a)Biochem. Biophys. Res. Commun.,82, 1.PubMedCrossRefGoogle Scholar
  19. Singh, R. P. and Setlow, P. (1978b)J. Bacteriol.,134, 353.PubMedGoogle Scholar
  20. Singh, R. P. and Setlow, P. (1979a)J. Bacteriol.,137, 1024.PubMedGoogle Scholar
  21. Singh, R. P. and Setlow, P. (1979b)J. Bacteriol.,139, 889.PubMedGoogle Scholar
  22. Watabe, K. and Freese, E. (1979)J. Bacteriol.,137, 773.PubMedGoogle Scholar
  23. Weber, K. and Osborne, M. (1969)J. Biol. Chem.,244, 4406.PubMedGoogle Scholar
  24. Whitaker, J. R. (1963)Anal. Chem.,35, 1950.CrossRefGoogle Scholar

Copyright information

© Indian Academy of Sciences 1982

Authors and Affiliations

  • Ravendra Pal Singh
    • 1
  1. 1.Department of BiochemistryUniversity of Connecticut, Health CenterFarmingtonUSA

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