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The basis for an apparent auxotrophy for reduced sulphur metabolites in sF− mutants of Aspergillus nidulans

Published online by Cambridge University Press:  14 April 2009

Herbert N. Arst Jr
Herbert N. Arst Jr
Affiliation:
Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, England
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sF− mutants of Aspergillus nidulans are subject to toxicity by a metabolite derived from sulphate but are not blocked in cysteine biosynthesis. Bearing in mind the unavoidable presence of sulphate in agar-solidified media, their apparent auxotrophy for thiosulphate, L-cysteine or L-methionine stems from the ability of these reduced sulphur-containing metabolites to repress, directly or indirectly, the syntheses of sulphate permease and the enzymes of sulphate assimilation, thereby preventing synthesis of the toxic metabolite.

Information

Type
Short paper
Information
Genetics Research , Volume 30 , Issue 2 , October 1977 , pp. 207 - 210
Copyright
Copyright © Cambridge University Press 1977

References

REFERENCES

Arst, H. N. Jr. (1968). Genetic analysis of the first steps of sulphate metabolism in Aspergillus nidulans. Nature 219, 268–270.Google Scholar
Arst, H. N. Jr. (1971). Mutants of Aspergillus nidulans unable to use choline-O-sulphate. Genetical Research 17, 273–277.CrossRefGoogle Scholar
Arst, H. N. Jr. & Macdonald, D. W. (1975). A gene cluster in Aspergillus nidulans with an internally located cis-acting regulatory region. Nature 254, 26–31.Google Scholar
Bal, J., Maleszka, R., Stepien, P. & Cybis, J. (1975). Subcellular mislocation of cysteine synthase in a cysteine auxotroph of Aspergillus nidulans. Federation of European Biochemical Societies Letters 58, 164–166.CrossRefGoogle Scholar
Gravel, R. A. (1976). Choline-O-sulphate utilization in Aspergillus nidulans. Genetical Research 28, 261–276.CrossRefGoogle ScholarPubMed
Gravel, R. A., Käfer, E., Niklewicz-Borkenhagen, A. & Zambryski, P. (1970). Genetic and accumulation studies in sulfite-requiring mutants of Aspergillus nidulans. Canadian Journal of Genetics and Cytology 12, 831–840.CrossRefGoogle ScholarPubMed
Lukaszkiewicz, Z. & Paszewski, A. (1976). Hyper-repressible operator-type mutant in sulphate permease gene of Aspergillua nidulans. Nature 259, 337–338.CrossRefGoogle Scholar
Morris, N. R. (1975). Mitotic mutants of Aspergillus nidulans. Genetical Research 26, 237–254.Google Scholar
Orsi, B. A. & Spencer, B. (1964). Choline sulphokinase (sulphotransferase). Journal of Biochemistry (Tokyo) 56, 81–91.Google Scholar
Paszewski, A. & Grabski, J. (1974). Regulation of S-amino acids biosynthesis in Aspergillus nidulans. Role of cysteine and/or homocysteine as regulatory effectors. Molecular and General Genetics 132, 307–320.Google Scholar
Paszewski, A. & Grabski, J. (1975). Enzymatic lesions in methionine mutants of Aspergillus nidulans: role and regulation of an alternative pathway for cysteine and methionine synthesis. Journal of Bacteriology 124, 893–904.CrossRefGoogle ScholarPubMed
Pieniazek, N. J., Bal, J., Balbin, E. & Stepien, P. P. (1974). An Aspergillus nidulans mutant lacking serine transacetylase: evidence for two pathways of cysteine biosynthesis. Molecular and General Genetics 132, 363–366.Google Scholar
Pieniazek, N. J., Kowalska, I. M. & Stepien, P. P. (1973). Deficiency in methionine adenosyltransferase resulting in limited repressibility of methionine biosynthetic enzymes in Aspergillus nidulans. Molecular and General Genetics 126, 367–374.CrossRefGoogle ScholarPubMed
Pieniazek, N. J., Stepien, P. P. & Paszewski, A. (1973). An Aspergillus nidulans mutant lacking cystathionine β-synthase: identity of L-serine sulfhydrylase with cystathionine β-synthase and its distinctness from O-acetyl-L-serine sulfhydrylase. Biochimica et Biophysica Acta 297, 37–47.Google Scholar
Stepien, P. P., Pieniazek, N. J., Bal, J. & Morzycka, E. (1975). Cysteine biosynthesis in Aspergillus nidulans. Acta Microbiologica Polonica A 7, 201–210.Google Scholar
Yoshimoto, A., Nakamura, T. & Sato, R. (1967). Isolation from Aspergillus nidulans of a protein catalysing the reduction of sulfite by reduced viologen dyes. Journal of Biochemistry (Tokyo) 62, 756–766.CrossRefGoogle ScholarPubMed
Kaji, A. & Gregory, J. D. (1959). Mechanism of sulfurylation of choline. Journal of Biological Chemistry 234, 3007–3009.Google Scholar