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Glutamic dehydrogenase in revertants of am mutants in neurospora

Published online by Cambridge University Press:  14 April 2009

David R. Stadler
David R. Stadler
Affiliation:
Department of Genetics, University of Washington, Seattle, Washington 98105
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Five allelic mutants of Neurospora which lack glutamic dehydrogenase (am mutants) were induced to revert with ultra-violet. The glutamic dehydrogenase produced by the revertants was compared to that of wild-type. Several distinct classes of revertants could be distinguished by these tests. However, genetic analysis showed that all the reversions resulted from events at or near the site of the original am mutation. The spectrum of reversion types depended on the nature of the am mutant employed. One mutant, which produces an am protein believed to be altered in its active site, yielded revertants which were all indistinguishable from wild-type. Another mutant, which produces a protein with a functional active site but altered folding properties, gave at least six classes of revertants which were different from wild-type.

Type
Research Article
Information
Genetics Research , Volume 7 , Issue 1 , February 1966 , pp. 18 - 31
Copyright
Copyright © Cambridge University Press 1966

References

REFERENCES

Barnett, W. E. & De Serres, F. J. (1963). Fixed genetic instability in Neurospora crassa. Genetics, 48, 717–723.CrossRefGoogle ScholarPubMed
Crick, F. H. C., Barnett, L., Brenner, S. & Watts-Tobin, R. J. (1961). General nature of the genetic codes for proteins, Nature, Lond. 192, 1227–1232.CrossRefGoogle ScholarPubMed
Drake, J. W. (1963). Properties of ultraviolet-induced rII mutants of bacteriophage T4. J. molec. Biol. 6, 268–283.CrossRefGoogle Scholar
Esser, K., DeMoss, J. A. & Bonner, D. M. (1960). Reverse mutations and enzyme heterogeneity. Z. VererbLehre, 91, 291–299.Google Scholar
Fincham, J. R. S. (1962). Genetically determined multiple forms of glutamic dehydrogenase in Neurospora crassa. J. molec. Biol. 4, 257–274.CrossRefGoogle ScholarPubMed
Fincham, J. R. S. & Coddinoton, A. (1963 a). Complementation at the am locus of Neurospora. crassa: a reaction between different mutant forms of glutamate dehydrogenase. J. molec. Biol. 6, 361–373.CrossRefGoogle Scholar
Fincham, J. R. S. & Coddington, A. (1963 b). The mechanism of complementation between am mutants of Neurospora crassa. Cold Spring Harb. Symp. quant. Biol. 28, 517–527.Google Scholar
Fincham, J. R. S. & Stadler, D. R. (1964). Complementation relationships of Neurospora am mutants in relation to their formation of abnormal varieties of glutamate dehydrogenase. Genet. Res. (in press).Google Scholar
Freese, E. (1963). Molecular mechanism of mutations. In Molecular Genetics, part I (Taylor, J. H., ed.), pp. 207–269. New York: Academic Press.Google Scholar
Giles, N. H. (1958). Mutations at specific loci in Neurospora. Proc. X Int. Cong. Genetics, 1, 261–279.Google Scholar
Giles, N. H., Partridge, C. W. H. & Nelson, N. J. (1957). The genetic control of anenylo-succinase in Neurospora crassa. Proc. natn. Acad. Sci. U.S.A. 43, 305–317.Google Scholar
Henning, U. & Yanofsky, C. (1962). Amino acid replacements associated with reversion and recombination within the A gene. Proc. natn. Acad. Sci. U.S.A. 48, 1497–1504.Google Scholar
Jinks, J. L. (1961). Internal suppressors of the h111 and tu45 mutants of bacteriophage T4. Heredity, Lond. 16, 241–254.Google Scholar
Lester, H. E. & Gross, S. R. (1959). Efficient method for selection of auxotrophic mutants of Neurospora. Science, N. Y. 129, 572.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosenbrough, N. J., Farr, N. J. & Randall, R. J. (1951). Protein measurements with the Folin phenol reagent. J. biol. Chem. 193, 265.CrossRefGoogle ScholarPubMed
Pateman, J. A. & Fincham, J. R. S. (1964). Complementation and enzyme studies of rever-tants induced in an am mutant of Neurospora crassa. Genet. Res. (in press).Google Scholar
Sundaram, T. K. & Fincham, J. R. S. (1964). A mutant enzyme in Neurospora interconvertible between electrophoretically distinct active and inactive forms. J. molec. Biol. (in press).Google Scholar
Yanofsky, C., Helinski, D. R. & Maling, B. D. (1961). The effects of mutation on the composition and properties of the A protein of Escherichia coli tryptophan synthetase. Cold Spring Harb. Symp. quant. Biol. 26, 11–24.Google Scholar