Arginaseless Neurospora : Genetics, Physiology, and Polyamine Synthesis

Author:

Davis Rowland H.1,Lawless Mary B.1,Port Loretta A.1

Affiliation:

1. Department of Botany, University of Michigan, Ann Arbor, Michigan 48104

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference21 articles.

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2. Sorbose toxicity;Brockman H. E.;Neurospora. Amer. J. Bot.,1964

3. The catabolism of L-arginine by Neurospora crassa;Castafieda M.;Biochim. Biophys. Acta,1967

4. Dosage des N-carbamoylderives d'acides amines par la diacetylmonoxime;Crokaert R.;Bull. Soc. Chim. Biol.,1958

5. A mutant form of ornithine transcarbamylase found in a strain of Neurospora carrying a pyrimidine-proline suppressor gene;Davis R. H.;Arch. Biochem. Biophys.,1962

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