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Amitrole Interference with Adenine-2-14C Metabolism by Saccharomyces cerevisiae

Published online by Cambridge University Press:  12 June 2017

J. L. Hilton  and
P. C. Kearney
J. L. Hilton
Affiliation:
Crops Research Division, Agricultural Research Service, U. S. Department of Agriculture, Beltsville, Maryland
P. C. Kearney
Affiliation:
Crops Research Division, Agricultural Research Service, U. S. Department of Agriculture, Beltsville, Maryland
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Abstract

Metabolic incorporation of adenine-2-14C by Saccharomyces cerevisiae was examined for alterations produced by 3-amino-1,2,4-triazole (amitrole) and histidine. The radioactivity recovered from cells after a 4-hour incubation was found predominantly in ethanol-insoluble components (nucleic acids and proteins) of untreated cultures. Amitrole inhibited incorporation of 14C into insoluble components. Carbon-labeled imidazoleglycerol phosphate, a precursor of histidine, and labeled imidazoleglycerol accumulated in the ethanol-soluble fraction of amitrole treated cells. Imidazoleglycerol accumulated in the external medium. Histidine prevented 14C incorporation into the hot trichloroacetic acid-insoluble residue (protein), prevented amitrole-induced imidazoleglycerol and imidazoleglycerol phosphate accumulation, and circumvented amitrole inhibition of 14C incorporation into the hot trichloroacetic acid-soluble (nucleic acids) fraction.

Type
Research Article
Information
Weeds , Volume 13 , Issue 1 , January 1965 , pp. 22 - 25
Copyright
Copyright © 1965 Weed Science Society of America 

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References

Literature Cited

1. Ames, B. N. and Hartman, P. E. 1962. Genes, enzymes, and control mechanisms in histidine biosynthesis, pp. 321–345. In The molecular basis of neoplasia. University of Texas Press, Austin, Texas.Google Scholar
2. Ames, B. N. and Mitchell, H. K. 1952. The paper chromatography of imidazoles. J. Am. Chem. Soc. 74:252–253.Google Scholar
3. Ames, B. N. and Mitchell, H. K. 1954. The biosynthesis of histidine. Imidazoleglycerol phosphate, imidazoleacetol phosphate and histidinol phosphate. J. Biol. Chem. 212:687–696.Google Scholar
4. Benson, A. A., Bassham, J. A., Calvin, M., Goodale, T. C., Haas, V. A., and Stepka, W. 1950. The path of carbon in photosynthesis. V. Paper chromatography and radioautography of the products. J. Am. Chem. Soc. 72:1710–1718.Google Scholar
5. Ezekiel, D. H. 1964. Intracellular charging of soluble ribonucleic acid in Escherichia coli subjected to isoleucine starvation and chloramphenicol treatment. Biochem. Biophys. Research Commun. 14:64–68.Google Scholar
6. Haemmerling, J. 1963. Nucleo-cytoplasmic interactions in Acetabularia and other cells. Ann. Rev. Plant Physiol. 14: 65–92.Google Scholar
7. Hilton, J. L. 1960. Effect of histidine on the inhibitory action of 3-amino-1,2,4-triazole. Weeds 8:392–396.Google Scholar
8. Hilton, J. L., Jansen, L. L., and Gentner, W. A. 1958. Betaalanine protection of yeast growth against the inhibitory action of several chlorinated aliphatic acid herbicides. Plant Physiol. 33:43–45.Google Scholar
9. Hilton, J. L., Jansen, L. L., and Hull, H. M. 1963. Mechanisms of herbicide action. Ann. Rev. Plant Physiol. 14:353–384.Google Scholar
10. King, T. E. and Cheldelin, V. H. 1948. Pantothenic acid studies. IV. Propionic acid and β-alanine utilization. T. Biol. Chem. 174:273–279.Google Scholar
11. Klopotowski, T. and Hulanicka, D. 1963. Imidazoleglycerol accumulation by yeast resulting from the inhibition of histidine biosynthesis by 3-amino-1,2,4-triazole. Acta Biochimica Polonica 10:209–218.Google Scholar
12. Kurland, C. G. and Maaloe, O. 1962. Regulation of ribosomal and transfer RNA synthesis. J. Mol. Biol. 4:193–210.Google Scholar
13. Roberts, R. B., Abelson, P. H., Cowie, D. B., Bolton, E. T., and Britten, R. J. 1957. Studies of biosynthesis in Escherichia coli . Carnegie Institution of Washington Publication 607, 2nd printing, Washington, D. C. Google Scholar
14. Smith, D. W. E. and Ames, B. N. 1964. Intermediates in the early steps of histidine biosynthesis. T. Biol. Chem. 239: 1848–1855.Google Scholar
15. Stent, G. S. and Brenner, S. 1961. A genetic locus for the regulation of ribonucleic acid synthesis. Proc. Nat. Acad Sci. 47:2005–2014.CrossRefGoogle ScholarPubMed
16. Tabor, H. 1957. Isolation and determination of histidine and related compounds, pp. 623–635. In Colowick, S. P. and Kaplan, N. O. (ed.) Methods in enzymology, Vol. III. Academic Press, Inc., New York, New York.Google Scholar
17. Tissieres, A., Bourgeois, S., and Gros, F. 1963. Inhibition of RNA polymerase by RNA. J. Mol. Biol. 7:100–103.Google Scholar
18. Weyter, F. W. and Broquist, H. P. 1960. Interference with adenine and histidine metabolism in microorganisms by aminotriazole. Biochem. Biophys. Acta. 40:567–569.Google Scholar