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PMID: 838690 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Control of arginine utilization in Neurospora.

Journal of bacteriology ·Vol. 129 ·No. 2 ·1977-02-00 ·Pages 866-73

Weiss RL, Davis RH

Abstract

The response of Neurospora to changes in the availibility of exogenous arginine was investigated. Upon addition of arginine to the growth medium, catabolism is initiated within minutes. This occurs prior to expansion of the arginine pool or augmentation of catabolic enzyme levels. (Basal levels are approximately 25% of those found during growth in arginine-supplemented medium.) Catabolism of arginine is independent of protein synthesis, indicating that the catabolic enzymes are active but that arginine is not available for catabolism unless present in the medium. Upon exhaustion of the supply of exogenous arginine, catabolism ceases abruptly, despite an expanded arginine pool and induced levels of the catabolic enzymes. The arginine pool supports protein synthesis until the cells regain their normal capacity for endogenous arginine synthesis. These observations, combined with the known small level of induction of arginine catabolic enzymes, non-repressibility of most biosynthetic enzymes, and vesicular localization of the bulk of the arginine pool, suggest that compartmentation plays a significant role in controlling arginine metabolism in Neurospora.

MeSH Terms
Arginase/metabolism Arginine/biosynthesis,metabolism Fungal Proteins/biosynthesis Mutation Neurospora/enzymology,metabolism Urea/biosynthesis
Chemicals
Fungal Proteins Urea Arginine Arginase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Weiss R L
Davis R H
References (22)
22 references, click to expand
  1. A KINETIC STUDY OF THE ASSIMILATION OF (15N)-AMMONIA AND THE SYNTHESIS OF AMINO ACIDS IN AN EXPONENTIALLY GROWING CULTURE OF CANDIDA UTILIS.
    Proc R Soc Lond B Biol Sci. 1964 Feb 18;159:479-502 PMID: 14116016
  2. A model for protein synthesis.
    Nature. 1962 Mar 3;193:821-3 PMID: 13906416
  3. [Determination of N-carbamoyl derivatives of amino acids by diacetylmonoxime].
    Bull Soc Chim Biol (Paris). 1958;40(7-8):1093-106 PMID: 13596813
  4. [Incorporation of endogenous and exogenous amino acids into proteins of yeast].
    Ann Inst Pasteur (Paris). 1958 Jul;95(1):73-87 PMID: 13545636
  5. Determination of creatine, creatinine, arginine, guanidinoacetic acid, guanidine, and methylguanidine in biological fluids.
    J Biol Chem. 1956 Sep;222(1):225-35 PMID: 13366996
  6. Colorimetric determination of carbamylamino acids and related compounds.
    J Biol Chem. 1954 Jul;209(1):145-50 PMID: 13192067
  7. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  8. Intracellular localization of ornithine and arginine pools in Neurospora.
    J Biol Chem. 1973 Aug 10;248(15):5409-13 PMID: 4272157
  9. Intracellular localization of enzymes of arginine metabolism in Neurospora.
    J Biol Chem. 1973 Aug 10;248(15):5403-8 PMID: 4358616
  10. Mutants of Neurospora crassa deficient in ornithine-delta-transmainase.
    J Bacteriol. 1968 Aug;96(2):383-8 PMID: 5674052
  11. Arginaseless Neurospora: genetics, physiology, and polyamine synthesis.
    J Bacteriol. 1970 May;102(2):299-305 PMID: 5419257
  12. Use of external, biosynthetic, and organellar arginine by Neurospora.
    J Bacteriol. 1973 Jul;115(1):284-90 PMID: 4717516
  13. Acetylglutamate kinase: a feedback-sensitive enzyme of arginine biosynthesis in Neurospora.
    Biochem Biophys Res Commun. 1974 Sep 23;60(2):629-34 PMID: 4371786
  14. Characterization of amino acid pools in the vacuolar compartment of Saccharomyces cerevisiae.
    Arch Microbiol. 1974;101(1):45-57 PMID: 4374149
  15. Regulation of arginase activity by intermediates of the arginine biosynthetic pathway in Neurospora crassa.
    J Bacteriol. 1972 Jun;110(3):870-7 PMID: 4260560
  16. Organization and control in the arginine biosynthetic pathway of Neurospora.
    J Bacteriol. 1975 Jul;123(1):196-202 PMID: 166979
  17. Metabolic compartmentation: symbiotic, organellar, multienzymic, and microenvironmental.
    Annu Rev Microbiol. 1974;28(0):61-83 PMID: 4611335
  18. The induction of urea carboxylase and allophanate hydrolase in Saccharomyces cerevisiae.
    J Biol Chem. 1973 Sep 10;248(17):6203-9 PMID: 4580053
  19. The induction of arginase in Saccharomyces cerevisiae.
    J Biol Chem. 1973 Sep 10;248(17):6197-202 PMID: 4580052
  20. Compartmentation of free valine and its relation to protein turnover in perfused rat liver.
    J Biol Chem. 1972 May 10;247(9):2776-84 PMID: 5025099
  21. Compartmentation and control of arginine metabolism in Neurospora.
    J Bacteriol. 1976 Jun;126(3):1173-9 PMID: 947887
  22. The accumulation of argininosuccinate in Neurospora crassa. II. Inhibition of arginyl-tRNA synthesis by argininosuccinate.
    Biochim Biophys Acta. 1967 Aug 22;145(1):146-52 PMID: 6053229
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1977-02-00
Pages
866-73
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC235023
Subset
IM
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