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Genetics of nitrate reductase in Ustilago maydis

Published online by Cambridge University Press:  14 April 2009

C. M. Lewis  and
J. R. S. Fincham
C. M. Lewis
Affiliation:
The John Innes Institute, Bayfordbury, Hertford, Herts, and The Department of Genetics, University of Leeds
J. R. S. Fincham
Affiliation:
The John Innes Institute, Bayfordbury, Hertford, Herts, and The Department of Genetics, University of Leeds
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Mutants of Ustilago maydis have been isolated both, deficient and derepressed for nitrate reduction. Those deficient in enzyme fall into six groups, one of which is the structural gene. Enzyme which has proved to be more labile than that of wild-type has been isolated from a temperature-sensitive mutant at this locus. All the mutants in the structural gene have xanthine dehydrogenase activity and the situation closely parallels that of Aspergillus nidulans.

The derepressed mutants fall into four complementation groups and all are partially derepressed in that they are further inducible by nitrate. Full derepression can be conferred by induction of a second mutation. In one analysed case the second reinforcing mutation proved to be pheno-typically similar to the first one when separated from it.

Type
Research Article
Information
Genetics Research , Volume 16 , Issue 2 , October 1970 , pp. 151 - 163
Copyright
Copyright © Cambridge University Press 1970

References

REFERENCES

Adhya, S., Cleary, P. & Campbell, A. (1968). A deletion analysis of prophage λ and adjacent genetic regions. Proceedings of the National Academy of Sciences of the United States of America 61, 956–962.CrossRefGoogle ScholarPubMed
Arst, H. N. & Cove, D. J. (1969). Meihylammonium resistance in Aapergillus nidulans. Journal of Bacteriology 98, 1284–1293.CrossRefGoogle Scholar
Azoulay, E., Puig, J. & Pichinoty, F. (1967). Alteration of respiratory particles by mutation in E. coli. K 12. Biochemical and Biophysical Research Communications 27, 270–274.CrossRefGoogle Scholar
Bnssey, A. H. (1966). Ph.D. Thesis, University of Bristol.Google Scholar
Cove, D. J. (1969). Evidence for a near limiting intracellular concentration of a regulator. Nature, London 224, 272–273.CrossRefGoogle ScholarPubMed
Cove, D. J. (1967). Kinetic studies of the induction of nitrate reduciase and cytochrome-c reduciase in the fungus Aspergillus nidulans. Biochemical Journal 104, 1033–1039.CrossRefGoogle Scholar
Cove, D. J. (1966). The induction and repression of nitrate reduciase in the fungus Aspergillus nidulans. Biochimica et biophysica acta 113, 51–56.CrossRefGoogle Scholar
Cove, D. J. & Pateman, J. A. (1969). Autoregulation of the synthesis of nitrate reduciase in Aspergillus nidulans. Journal of Bacteriology 97, 1374–1378.CrossRefGoogle Scholar
Fink, G. R. & Roth, J. R. (1968). Histidine regulatory mutants in S. typhimurium. IV. Dominance studies. Journal of Molecular Biology 33, 533–547.CrossRefGoogle Scholar
Hewitt, D. J. & Afridi, M. M. R. K. (1959). Adaptive synthesis of nitrate reduciase in higher plants. Nature, London 183, 57–58.CrossRefGoogle Scholar
Holliday, R. (1961 a). The genetics of Ustilago maydis. Genetical Research 2, 204–230.CrossRefGoogle Scholar
Holliday, R. (1961 b). Induced mitotic crossing over in Ustilago maydis. Genetical Research 2, 231–248.CrossRefGoogle Scholar
Lester, H. E. & Gross, S. R. (1959). An efficient method for selection of auxotrophic muianis in neurospora. Science, New York 129, 572.CrossRefGoogle ScholarPubMed
Lewis, C. M. & Fincham, J. R. S. (1970). Regulation of nitraie reduciase in the Basidio-myceie Ustilago maydis. Journal of Bacteriology (in ihe Press).CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. H., Farr, A. L. & Randall, R. J. (1951). Proiein measurements with ihe Folin-Phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle Scholar
Morris, I. & Syrett, J. (1963). Development of nitrate reduciase in Chlorella and its repression by ammonium. Archiv für Mikrobiologie 47, 32–41.CrossRefGoogle Scholar
Nason, A. & Evans, H. J. (1953). TPNH-nitraie reduciase in Neurospora. Journal of Biological Chemistry 202, 655–673.CrossRefGoogle Scholar
Nicholas, D. J. D. & Nason, A. (1955 a). Diphosphopyridine nucleoiide nitrate reduciase from E. coli. Journal of Bacteriology 69, 580–583.CrossRefGoogle Scholar
Nicholas, D. J. D. & Nason, A. (1955 b). Role of molybdenum as a consiiiueni of nitrate reduciase from soybean leaves. Plant Physiology 30, 135–138.CrossRefGoogle Scholar
Pateman, J. A., Cove, D. J., Rever, B. M. & Roberts, D. B. (1964). A common co-factor for nitrate reduciase and xanthine dehydrogenase which also regulates the synihesis of nitrate reduciase in Aspergillus nidulans. Nature, London 201, 58–60.CrossRefGoogle Scholar
Patemau, J. A., Rever, B. M. & Cove, D. J. (1965). Conirol of nitrate induced enzymes in Aspergillus nidulans. Heredity 20, 650.Google Scholar
Pateman, J. A. & Cove, D. J. (1967 a). The regulation of nitrate reduciase in Aspergillus nidulans. Nature, London 215, 1234–1237.CrossRefGoogle Scholar
Pateman, J. A., Rever, B. M. & Cove, D. J. (1967 b). Genetic and biochemical studies of nitraie reduction in Aspergillus nidulans. Biochemical Journal 104, 103–111.CrossRefGoogle ScholarPubMed
Pichinoty, F. & Metenier, G. (1966). Coniribution a l'etude de la nitraie reduciase assimi-lairice d'une levure. Annales de l' Institut Pasteur 111, 282–313.Google Scholar
Rijven, A. H. G. C. (1958). Effects of some inorganic niirogenous subsiances on growth and nitrogen assimilation of young plant embryos in vitro. Australian Journal of Biological Sciences 11, 142–154.CrossRefGoogle Scholar
Sadana, J. C. & McElroy, W. D. (1962). Nitrate reductase from Achromobacter fischeri. Purification and properties, ihe function of flavines and cyiochrome. Archives of Biochemistry and Biophysics 67, 16–34.CrossRefGoogle Scholar
Showe, M. K. & DsMoss, J. A. (1968). Localization of and regulation of synthesis of nitrate reduciase in E. coli. Journal of Bacteriology 95, 1305.CrossRefGoogle Scholar
Snow, R. (1966). An enrichment method for auxotrophic yeast mutants using the antibiotic nystatin. Nature, London 211, 206–207.CrossRefGoogle ScholarPubMed
Sorger, G. J. (1963). TPNH cytochrome-c reduciase and nitrate redactase in mutant and wild-type neurospora and aspergillus. Biochemical and Biophysical Research Communications 12, 395–401.CrossRefGoogle Scholar
Sorger, G. J. (1966). Nitrate reduciase electron transport systems in mutant and wild-type strains of neurospora. Biochimica et biophysica acta 118, 484–494.CrossRefGoogle Scholar
Sorger, G. J. & Giles, N. H. (1965). Genetic control of nitrate reduciase in neurospora. Genetics 52, 777–788.CrossRefGoogle Scholar
Yudkin, M. O. (1966). Pritein synthesis by long lived mRNA in bacieria. Biochemical Journal 100, 501–506.CrossRefGoogle Scholar
Tang, P. & Wu, H. (1957). Adapiive formation of nitraie reduciase in rice seedlings. Nature, London 179, 1355–1356.CrossRefGoogle Scholar