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. 1970 May;102(2):299–305. doi: 10.1128/jb.102.2.299-305.1970

Arginaseless Neurospora: Genetics, Physiology, and Polyamine Synthesis

Rowland H Davis 1, Mary B Lawless 1, Loretta A Port 1
PMCID: PMC247551  PMID: 5419257

Abstract

Four arginaseless mutants of Neurospora crassa have been isolated. All carry mutations which lie at a single locus, aga, on linkage group VIIR. A study of aga strains shows the arginase reaction to be the major, perhaps the only, route of arginine consumption in Neurospora other than protein synthesis. Ornithine-δ-transaminase, the second enzyme of the arginine catabolic pathway, is present and normally inducible by arginine in aga strains, and ornithine transcarbamylase, an enzyme of arginine synthesis, also has normal activity. Arginine inhibits the growth of aga strains. The inhibition can be reversed by spermidine, putrescine (1,4-diaminobutane), or ornithine. The results suggest that ornithine is the major source of the putrescine moiety of polyamines in Neurospora, and that putrescine is an essential growth factor for this organism. The inhibition of aga strains by arginine can be attributed to feedback inhibition of ornithine synthesis by arginine, combined with the complete lack of ornithine normally provided by the arginase reaction.

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Selected References

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

  1. ABELSON P. H., VOGEL H. J. Amino acid biosynthesis in Torulopsis utilis and Neurospora crassa. J Biol Chem. 1955 Mar;213(1):355–364. [PubMed] [Google Scholar]
  2. ANDERTON J. I., LOCKE D. J. Extraction of pigment from cooked cured-meat products. Nature. 1955 May 7;175(4462):818–819. doi: 10.1038/175818b0. [DOI] [PubMed] [Google Scholar]
  3. CROKAERT R., SCHRAM E. Dosage des N-carbamoyldérivés d'acides aminés par la diacétylmonoxime. Bull Soc Chim Biol (Paris) 1958;40(7-8):1093–1106. [PubMed] [Google Scholar]
  4. Castañeda M., Martuscelli J., Mora J. The catabolism of L-arginine by Neurospora crassa. Biochim Biophys Acta. 1967 Jul 25;141(2):276–286. doi: 10.1016/0304-4165(67)90102-x. [DOI] [PubMed] [Google Scholar]
  5. DAVIS R. H. A mutant form of ornithine transcarbamylase found in a strain of Neurospora carrying a pyrimidine-proline suppressor gene. Arch Biochem Biophys. 1962 Apr;97:185–191. doi: 10.1016/0003-9861(62)90063-2. [DOI] [PubMed] [Google Scholar]
  6. Davis R. H., Mora J. Mutants of Neurospora crassa deficient in ornithine-delta-transmainase. J Bacteriol. 1968 Aug;96(2):383–388. doi: 10.1128/jb.96.2.383-388.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davis R. H. Utilization of exogenous and endogenous ornithine by Neurospora crassa. J Bacteriol. 1968 Aug;96(2):389–395. doi: 10.1128/jb.96.2.389-395.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hirshfield I. N., Rosenfeld H. J., Leifer Z., Maas W. K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J Bacteriol. 1970 Mar;101(3):725–730. doi: 10.1128/jb.101.3.725-730.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KORITZ S. B., COHEN P. P. Colorimetric determination of carbamylamino acids and related compounds. J Biol Chem. 1954 Jul;209(1):145–150. [PubMed] [Google Scholar]
  10. Kolmark H. G. Genetic studies of urease mutants in Neurospora crassa. Mutat Res. 1969 Jul-Aug;8(1):51–63. doi: 10.1016/0027-5107(69)90140-7. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Messenguy F., Wiame J. -M. The control of ornithinetranscarbamylase activity by arginase in Saccharomyces cerevisiae. FEBS Lett. 1969 Apr;3(1):47–49. doi: 10.1016/0014-5793(69)80093-1. [DOI] [PubMed] [Google Scholar]
  13. Morris D. R., Jorstad C. M. Isolation of conditionally putrescine-deficient mutants of Escherichia coli. J Bacteriol. 1970 Mar;101(3):731–737. doi: 10.1128/jb.101.3.731-737.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Piotrowska M., Sawicki M., Weglenski P. Mutants of the arginine-proline pathway in Aspergillus nidulans. J Gen Microbiol. 1969 Feb;55(2):301–305. doi: 10.1099/00221287-55-2-301. [DOI] [PubMed] [Google Scholar]
  15. TABOR H., TABOR C. W. SPERMIDINE, SPERMINE, AND RELATED AMINES. Pharmacol Rev. 1964 Sep;16:245–300. [PubMed] [Google Scholar]
  16. Woodward V. W., De Zeeuw J. R., Srb A. M. THE SEPARATION AND ISOLATION OF PARTICULAR BIOCHEMICAL MUTANTS OF NEUROSPORA BY DIFFERENTIAL GERMINATION OF CONIDIA, FOLLOWED BY FILTRATION AND SELECTIVE PLATING. Proc Natl Acad Sci U S A. 1954 Mar;40(3):192–200. doi: 10.1073/pnas.40.3.192. [DOI] [PMC free article] [PubMed] [Google Scholar]

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