Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Jun;82(12):4105–4109. doi: 10.1073/pnas.82.12.4105

Distinct roles of putrescine and spermidine in the regulation of ornithine decarboxylase in Neurospora crassa.

R H Davis, G N Krasner, J J DiGangi, J L Ristow
PMCID: PMC397943  PMID: 3159019

Abstract

We wished to identify metabolic signals governing changes in ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activity in Neurospora crassa. By manipulations of the ornithine supply and by the use of inhibitors of the polyamine pathway, we found that spermidine negatively governs formation of active ornithine decarboxylase and that putrescine promotes inactivation of the enzyme. Direct addition of putrescine or spermidine to cycloheximide-treated cells confirmed the role of putrescine in enzyme inactivation and showed that spermidine had no effect on this process. Increases in ornithine decarboxylase activity caused by blocking spermidine synthesis occurred prior to a significant decrease in the spermidine pool. This is consistent with our previous finding that only 10-20% of the spermidine pool is freely diffusible within N. crassa cells. We presume that only this small fraction of the pool is active in regulation.

Full text

PDF
4105

Images in this article

4108Image
on p.4108

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Atmar V. J., Kuehn G. D. Phosphorylation of ornithine decarboxylase by a polyamine-dependent protein kinase. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5518–5522. doi: 10.1073/pnas.78.9.5518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Basabe J. R., Lee C. A., Weiss R. L. Enzyme assays using permeabilized cells of Neurospora. Anal Biochem. 1979 Jan 15;92(2):356–360. doi: 10.1016/0003-2697(79)90670-5. [DOI] [PubMed] [Google Scholar]
  3. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  4. Canellakis E. S., Viceps-Madore D., Kyriakidis D. A., Heller J. S. The regulation and function of ornithine decarboxylase and of the polyamines. Curr Top Cell Regul. 1979;15:155–202. [PubMed] [Google Scholar]
  5. Cramer C. L., Davis R. H. Polyphosphate-cation interaction in the amino acid-containing vacuole of Neurospora crassa. J Biol Chem. 1984 Apr 25;259(8):5152–5157. [PubMed] [Google Scholar]
  6. Davis R. H., Lawless M. B., Port L. A. Arginaseless Neurospora: genetics, physiology, and polyamine synthesis. J Bacteriol. 1970 May;102(2):299–305. doi: 10.1128/jb.102.2.299-305.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davis R. H., Ristow J. L. Control of the ornithine cycle in Neurospora crassa by the mitochondrial membrane. J Bacteriol. 1983 Jun;154(3):1046–1053. doi: 10.1128/jb.154.3.1046-1053.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goodman I., Weiss R. L. Control of arginine metabolism in Neurospora: flux through the biosynthetic pathway. J Bacteriol. 1980 Jan;141(1):227–234. doi: 10.1128/jb.141.1.227-234.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hacker A. D., Tierney D. F., O'Brien T. K. Polyamine metabolism in rat lungs with oxygen toxicity. Biochem Biophys Res Commun. 1983 Jun 15;113(2):491–496. doi: 10.1016/0006-291x(83)91752-7. [DOI] [PubMed] [Google Scholar]
  10. Heller J. S., Chen K. Y., Kyriakidis D. A., Fong W. F., Canellakis E. S. The modulation of the induction of ornithine decarboxylase by spermine, spermidine and diamines. J Cell Physiol. 1978 Aug;96(2):225–234. doi: 10.1002/jcp.1040960211. [DOI] [PubMed] [Google Scholar]
  11. Hibasami H., Tanaka M., Nagai J., Ikeda T. Dicyclohexylamine, a potent inhibitor of spermidine synthase in mammalian cells. FEBS Lett. 1980 Jul 11;116(1):99–101. doi: 10.1016/0014-5793(80)80537-0. [DOI] [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. McCann P. P., Tardif C., Hornsperger J. M., Böhlen P. Two distinct mechanisms for ornithine decarboxylase regulation by polyamines in rat hepatoma cells. J Cell Physiol. 1979 May;99(2):183–190. doi: 10.1002/jcp.1040990204. [DOI] [PubMed] [Google Scholar]
  14. Mitchell J. L., Augustine T. A., Wilson J. M. Protein factor which induces conversion between Physarum ornithine decarboxylase forms in vitro. Biochim Biophys Acta. 1981 Jan 15;657(1):257–267. doi: 10.1016/0005-2744(81)90149-2. [DOI] [PubMed] [Google Scholar]
  15. Mitchell J. L., Carter D. D., Rybski J. A. Control of ornithine decarboxylase activity in Physarum by polyamines. Eur J Biochem. 1978 Dec;92(2):325–331. doi: 10.1111/j.1432-1033.1978.tb12751.x. [DOI] [PubMed] [Google Scholar]
  16. Paulus T. J., Cramer C. L., Davis R. H. Compartmentation of spermidine in Neurospora crassa. J Biol Chem. 1983 Jul 25;258(14):8608–8612. [PubMed] [Google Scholar]
  17. Paulus T. J., Davis R. H. Metabolic sequestration of putrescine in Neurospora crassa. Biochem Biophys Res Commun. 1982 Jan 15;104(1):228–233. doi: 10.1016/0006-291x(82)91963-5. [DOI] [PubMed] [Google Scholar]
  18. Paulus T. J., Davis R. H. Regulation of polyamine synthesis in relation to putrescine and spermidine pools in Neurospora crassa. J Bacteriol. 1981 Jan;145(1):14–20. doi: 10.1128/jb.145.1.14-20.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Paulus T. J., Kiyono P., Davis R. H. Polyamine-deficient Neurospora crassa mutants and synthesis of cadaverine. J Bacteriol. 1982 Oct;152(1):291–297. doi: 10.1128/jb.152.1.291-297.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pegg A. E., Conover C., Wrona A. Effects of aliphatic diamines on rat liver ornithine decarboxylase activity. Biochem J. 1978 Mar 15;170(3):651–660. doi: 10.1042/bj1700651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pegg A. E., Shuttleworth K., Hibasami H. Specificity of mammalian spermidine synthase and spermine synthase. Biochem J. 1981 Aug 1;197(2):315–320. doi: 10.1042/bj1970315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Persson L., Seely J. E., Pegg A. E. Investigation of structure and rate of synthesis of ornithine decarboxylase protein in mouse kidney. Biochemistry. 1984 Jul 31;23(16):3777–3783. doi: 10.1021/bi00311a033. [DOI] [PubMed] [Google Scholar]
  23. Pösö H., Guha S. K., Jänne J. Stabilization of ornithine decarboxylase in rat liver. Biochim Biophys Acta. 1978 Jun 9;524(2):466–473. doi: 10.1016/0005-2744(78)90185-7. [DOI] [PubMed] [Google Scholar]
  24. Stevens L., Winther M. D. Spermine, spermidine and putrescine in fungal development. Adv Microb Physiol. 1979;19:63–148. doi: 10.1016/s0065-2911(08)60198-8. [DOI] [PubMed] [Google Scholar]
  25. Tabor C. W., Tabor H. Polyamines. Annu Rev Biochem. 1984;53:749–790. doi: 10.1146/annurev.bi.53.070184.003533. [DOI] [PubMed] [Google Scholar]
  26. Tyagi A. K., Tabor C. W., Tabor H. Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity. J Biol Chem. 1981 Dec 10;256(23):12156–12163. [PubMed] [Google Scholar]
  27. Williams-Ashman H. G., Schenone A. Methyl glyoxal bis(guanylhydrazone) as a potent inhibitor of mammalian and yeast S-adenosylmethionine decarboxylases. Biochem Biophys Res Commun. 1972 Jan 14;46(1):288–295. doi: 10.1016/0006-291x(72)90661-4. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES