Biochemical and Genetic Studies on the Initial Events of Fruitbody Formation

  • Isao Uno
  • Tatsuo Ishikawa
Part of the Springer Series in Microbiology book series (SSMIC)

Abstract

The process of fruitbody formation in higher basidiomycetes involves the expression of a series of structural and regulatory genes required for the morphogenetic reactions. The first reaction necessary to initiate fruiting may be triggered by a genetic factor under certain environmental conditions. The incompatibility factors have been studied extensively since it has been shown that these factors regulate dikaryotization prerequisite to fruiting in the normal process of development (Raper, 1966; Raper and Raper, 1968). It is, however, known that fruiting is not limited to dikaryotic mycelia; monokaryotic mycelia produce fruitbodies under particular conditions such as aging, injury, or influence of some substances (Stahl and Esser, 1976). Various types of mutants that form fruitbodies on monokaryotic mycelia have also been found (Stahl and Esser, 1976). Study of monokaryotic fruiting has the advantage of dealing with a simple system of initiating fruiting free from the combination of incompatibility factors. We have made a series of experiments showing that adenosine 3′,5′-cyclic monophosphate (cyclic AMP) is one of the trigger substances in monokaryotic fruiting of Coprinus macrorhizus Rea f. microsporus Hongo. The present report describes the outline of the work and suggests a possible mechanism through which cyclic AMP exerts the effect on fruiting.

Keywords

Adenosine Fractionation Caffeine Adenine Theophylline 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Billar-Palasi, C., Larner, J.: Glycogen metabolism and glycolytic enzymes. Annu. Rev. Biochem. 39, 639–672 (1970).CrossRefGoogle Scholar
  2. Butcher, R. W., Sutherland, E. W.: Adenosine 3′,5′-phosphate in biological materials. I. Purification and properties of cyclic 3′,5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′,5′-phosphate in human urine. J. Biol. Chem. 237, 1244–1250 (1962).PubMedGoogle Scholar
  3. Gilman, A. G.: A protein binding assay for adenosine 3′,5′-cyclic monophosphate. Proc. Natl. Acad. Sci. USA 67, 305–312 (1970).PubMedCrossRefGoogle Scholar
  4. Khandelwal, R. L., Hamilton, LR.: Purification and properties of adenyl cyclase from Streptococcus salivarius. J. Biol. Chem. 246, 3297–3304 (1971).PubMedGoogle Scholar
  5. Raper, J. R.: Genetics of Sexuality in Higher Fungi. New York: Ronald Press 1966.Google Scholar
  6. Raper, J. R., Raper, C. A.: Genetic regulation of sexual morphogenesis in Schizophyllum commune. J. Elisha Mitchell Sci. Soc. 84, 267–273 (1968).Google Scholar
  7. Rubin, C. S., Rosen, O. M.: Protein phosphorylation. Annu. Rev. Biochem. 44, 831–887 (1975).PubMedCrossRefGoogle Scholar
  8. Stahl, U., Esser, K.: Genetics of fruitbody production in higher basidiomycetes. I. Monokaryotic fruiting and its correlation with dikaryotic fruiting in Polyporus ciliatus. Molec. Gen. Genet. 148, 183–197 (1976).CrossRefGoogle Scholar
  9. Steiner, A. L., Parker, C. W., Kipnis, D. M.: Radioimmunoassay for cyclic nucleotides. I. Preparation of antibodies and iodinated cyclic nucleotides. J. Biol. Chem. 247, 1106–1113 (1972).PubMedGoogle Scholar
  10. Uno, I., Ishikawa, T.: Chemical and genetical control of induction of monokaryotic fruiting bodies in Coprinus macrorhizus. Molec. Gen. Genet. 113, 228–239 (1971).CrossRefGoogle Scholar
  11. Uno, I., Ishikawa, T.: Purification and identification of the fruiting inducing substances in Coprinus macrorhizus. J. Bacteriol. 113, 1240–1248 (1973a).PubMedGoogle Scholar
  12. Uno, I., Ishikawa, T.: Metabolism of adenosine 3′,5′-cyclic monophosphate and induction of fruiting bodies in Coprinus macrorhizus. J. Bacteriol. 113, 1249–1255 (1973b).PubMedGoogle Scholar
  13. Uno, I., Ishikawa, T.: Presence of multiple protein kinase activities in Coprinus macrorhizus. Biochim. Biophys. Acta 334, 354–360 (1974a).Google Scholar
  14. Uno, I., Ishikawa, T.: Effect of glucose on the fruiting body formation and adenosine 3′,5′-cyclic monophosphate level in Coprinus macrorhizus. J. Bacteriol. 120, 96–100 (1974b).PubMedGoogle Scholar
  15. Uno, I., Ishikawa, T.: A biochemical basis of fruiting body formation in Coprinus macrorhizus. Proc. 1st. Inter. Congr. IAMS (Tokyo) 1, 313–321 (1975).Google Scholar
  16. Uno, I., Ishikawa, T.: Effect of cyclic AMP on glycogen Phosphorylase in Coprinus macrorhizus. Biochim. Biophys. Acta 452, 112–120 (1976).PubMedGoogle Scholar
  17. Uno, I., Ishikawa, T.: Effect of cyclic AMP on glycogen synthetase in Coprinus macrorhizus. J. Gen. Appl. Microbiol. 24, 193–197 (1978).CrossRefGoogle Scholar
  18. Uno, I., Yamaguchi, M., Ishikawa, T.: The effect of light on fruiting body formation and adenosine 3′,5′-cyclic monophosphate metabolism in Coprinus macrorhizus. Proc. Natl. Acad. Sci. USA 71, 479–483 (1974).PubMedCrossRefGoogle Scholar
  19. Walsh, D. A., Perkins, J. P., Krebs, E. G.: An adenosine 3′,5′-monophosphate dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243, 3763–3765 (1968).PubMedGoogle Scholar

Copyright information

© Springer-Verlag New York Inc. 1982

Authors and Affiliations

  • Isao Uno
  • Tatsuo Ishikawa

There are no affiliations available

Personalised recommendations