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A genetic analysis of CRM negative mutants at the td locus of Neurospora crassa

Published online by Cambridge University Press:  14 April 2009

S. Kaplan
Affiliation:
Department of Cellular Biology, University of California, San Diego, La Jolla, California, U.S.A.
Y. Suyama
Affiliation:
Department of Cellular Biology, University of California, San Diego, La Jolla, California, U.S.A.
D. M. Bonner
Affiliation:
Department of Cellular Biology, University of California, San Diego, La Jolla, California, U.S.A.
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The possibility that primary CRM isolates at the td locus of Neurospora crassa are multisite lesions has been examined. By comparing the behavior of primary CRM mutants to known multisite CRM mutants in the genetic tests of recombination and reversion, it can be concluded that primary CRM mutants are not multisite. The genetic implications of a CRM and CRM+ mutant have been discussed.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1963

References

REFERENCES

Ahmad, M. & Catcheside, D. G. (1960). Physiological diversity amongst tryptophan mutants in Neurospora crassa. Heredity, 15, 5564.CrossRefGoogle Scholar
Benzer, S. & Champe, S. P. (1962). A change from nonsense to sense in the genetic code. Proc. nat. Acad. Sci., Wash., 48, 11141121.CrossRefGoogle ScholarPubMed
Bonner, D. M., Suyama, Y. & DeMoss, J. (1960). Genetic fine structure and enzyme formation. Fed. Proc. 19, 926930.Google Scholar
DeMoss, J. & Bonner, D. M. (1959). Studies with normal and genetically altered tryptophan synthetase from Neurospora crassa. Proc. nat. Acad. Sci., Wash., 45, 14051412.CrossRefGoogle ScholarPubMed
Freese, , Elisabeth, B. (1961). Transitions and transversions induced by depurinating agents. Proc. nat. Acad. Sci., Wash., 47, 540545.CrossRefGoogle ScholarPubMed
Garen, A. (1960). Genetic control of the specificity of the bacterial enzyme, alkaline phosphatase. Symp. Soc. Gen. Microbiol., 10, 239247.Google Scholar
Henning, U. & Yanofsky, C. (1962). Amino acid replacements associated with reversion and recombination within the A gene. Proc. not. Acad. Sci., Wash., 48, 14971504.CrossRefGoogle ScholarPubMed
Kaplan, S., Suyama, Y. & Bonner, D. M. (1963). Manuscript in preparation. Fine structure analysis at the td locus of Neurospora crassa.Google Scholar
Lee, Nancy & Englesberg, E. (1962). Dual effects of structural genes in Escherichia coli. Proc. nat. Acad. Sci., Wash., 48, 335348.CrossRefGoogle ScholarPubMed
Rachmeler, M. & Yanofsky, C. (1961). Biochemical, immunological, and genetic studies with a new type of tryptophan synthetase mutant of Neurospora crassa. J. Bact. 81, 955963.CrossRefGoogle ScholarPubMed
Suskind, S. R., Yanofsky, C. & Bonner, D. M. (1955). Allelic strains of Neurospora lacking tryptophan synthetase: a preliminary immuno-chemical characterization. Proc. nat. Acad. Sci., Wash., 41, 577582.CrossRefGoogle Scholar
Suyama, Y. (1960). Effects of pyridoxal phosphate and serine in conversion of indoleglycerol-phosphate to indole by extracts from tryptophan mutants of Neurospora crassa. Biochem. & Biophys. Res. Comm. 3, 493499.CrossRefGoogle Scholar
Suyama, Y. (1962). Unpublished results.Google Scholar
Suyama, Y., Lacy, Ann & Bonner, D. M. (1963). Manuscript in preparation. Genetic map at the td locus.Google Scholar
Tsugita, A. & Fraenkel-Conrat, H. (1962). The composition of proteins of chemically evoked mutants of TMV RNA. J. mol. Biol. 4, 7382.CrossRefGoogle ScholarPubMed
Vogel, H. J. (1956). A convenient growth medium for Neurospora (Medium N). Microbiol. Genetics Bull. 13, 4243.Google Scholar
Woodward, V. W., DeZeeuw, J. R. & Srb, A. M. (1954). The separation and isolation of particular biochemical mutants of Neurospora by differential germination of conidia, followed by filtration and selective plating. Proc. nat. Acad. Sci., Wash., 40, 192200.CrossRefGoogle ScholarPubMed
Yanofsky, C. & Stadler, Joan (1958). The enzymatic activity associated with the protein immunologically related to tryptophan synthetase. Proc. nat. Acad. Sci., Wash., 44, 245253.CrossRefGoogle ScholarPubMed
Yanofsky, C. (1960). The tryptophan synthetase system. Bact. Rev. 24, 221245.CrossRefGoogle ScholarPubMed