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Mitochondrial mutagenesis in Saccharomyces cerevisiae: the origin of mit− mutants

Published online by Cambridge University Press:  14 April 2009

Aleksandra Putrament  and
Anna Ejchart
Aleksandra Putrament
Affiliation:
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Rakowiecka 36, 02-532 Warsaw, Poland
Anna Ejchart
Affiliation:
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Rakowiecka 36, 02-532 Warsaw, Poland

Summary

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Yeast cells contain many copies of mitochondrial (mit) genomes. The question we tried to answer was how mit− mutations occurring in one genome as a result of mutagenic treatment might yield homoplasmic mutant cells. Three processes were considered. First, that these cells originate by segregation of mutant and standard alleles during cell division. Secondly, that they originate through intracellular selection, for which cell division is not required. Thirdly, that recombination involving the mutant and standard alleles is non-reciprocal and unidirectional mit+ → mit− so that the mutant allele is spread into the entire population of mitochondrial genomes within a cell, thus making it homoplasmic mit−. The results indicate that the first process, although efficiently producing homoplasmic cells from heteroplasmic zygotes (for review see Birky, 1978), seems to play only a minor, if any, role in producing homoplasmic mutant progenies from mutagenized cells. The most important is the second process, that is, intracellular selection occurring in cells which have one or a few genomes carrying mit− mutations, while the remaining genomes are irreversibly damaged. The third process, unidirectional mit+ → mit− conversion, does not seem to play any part.

Type
Research Article
Information
Genetics Research , Volume 38 , Issue 3 , December 1981 , pp. 267 - 279
Copyright
Copyright © Cambridge University Press 1981

References

REFERENCES

Beale, G. H., Knowles, J. & Tait, A. (1972). Mitochondrial genetics in Paramecium. Nature 235, 396–397.CrossRefGoogle ScholarPubMed
Birky, C. W. Jr. (1973). On the origin of mitochondrial mutants: evidence for intracellular selection of mitochondria in the origin of antibiotic-resistant cells in yeast. Genetics 74, 421–432.CrossRefGoogle ScholarPubMed
Birky, C. W. (1978). Transmission genetics of mitochondria and chloroplast. Annual Review of Genetics 12, 471–512.CrossRefGoogle Scholar
Cabral, F., Solioz, M., Rudin, Y., Schatz, G., Clavilier, L. & Slonimski, P. P. (1978). Identification of the structural gene for yeast cytochrome c oxidase subunit II on mitochondrial DNA. The Journal of Biological Chemistry 253, 297–304.CrossRefGoogle ScholarPubMed
Dujon, B., Bolotin-Fukuhara, M., Coen, D., Deutsch, J., Netter, P., Slonimski, P. P. & Weill, L. (1976). Mitochondrial geneticsx. XI. Mutations at the mitochondrial locus omega affecting the recombination of mitochondrial genes in Saccharomyces cerevisiae. Molecular and General Genetics 143, 131–165.CrossRefGoogle ScholarPubMed
Dujon, B., Slonimski, P. P. & Weill, L. (1974). Mitochondrial genetics. IX: A model for recombination and segregation of mitochondrial genomes in Saccharomyces cerevisiae. Genetics 78, 415–437.CrossRefGoogle Scholar
Kotylak, Z. & Slonimski, P. P. (1977). Mitochondrial mutants isolated by a new screening method based upon the use of the nuclear mutation op1. In Mitochondria 1977. Genetics and biogenesis of mitochondria. Proceeding of a colloquium held at Schliersee, Germany, August 1977 (ed. Bandlow, W., Schweyen, R. J., Wolf, K. and Kaudewitz, F.), pp. 83–89. Berlin, New York: W. de Gruyter.CrossRefGoogle Scholar
Kovacova, V., Irmlerowa, J. & Kovac, L. (1968). Oxidative phosphorylation in yeast. IV. Combination of nuclear mutation affecting oxidase phosphorylation with cy toplasmic mutation to respiratory deficiency. Biochimica et Biophysica Acta 162, 157–163.CrossRefGoogle Scholar
Kruszewska, A. & Szczesniak, B. (1980). Construction of isomitochondrial and isonuclear strains for recombinational analysis of mitochondrial loci in S. cerevisiae. Genetical Research 35, 225–229.CrossRefGoogle Scholar
Putrament, A., Baranowska, H. & Prazmo, W. (1973). Induction by manganese of mitochondrial antibiotic resistance mutations in yeast. Molecular and General Genetics 126, 357–366.CrossRefGoogle ScholarPubMed
Putrament, A., Baranowska, H., Ejchart, A. & Prazmo, W. (1975). Manganese mutagenesis in yeast. A practical application of manganese for the induction of mitochondrial antibiotic-resistant mutations. Journal of General Microbiology 90, 265–270.CrossRefGoogle ScholarPubMed
Putrament, A., Polakowska, R., Baranowska, H. & Ejchart, A. (1976). On homozygotization of mitochondrial mutations in Saccharomyces cerevisiae. In Genetics and Biogenesis of Chloroplasts and Mitochondria (ed. Bucher, Th., Neupert, W., Sebald, W. and Werner, S.), pp. 415–418. Amsterdam: Elsevier/North Holland Biomedical Press.Google Scholar
Putrament, A., Baranowska, H., Ejchart, A. & Jachymczyk, W. (1977). Manganese mutagenesis in yeast. VI. Uptake, mitDNA replication and ER induction. Comparison with other divalent cations. Molecular and General Genetics 151, 69–76.CrossRefGoogle ScholarPubMed
Putrament, A., Baranowska, H., Ejchart, A. & Prazmo, W. (1978). Manganese mutagenesis in yeast. In Methods in Cell Biology, vol. 20, pp. 25–34. New York, San Francisco, London: Academic Press.Google Scholar
Queiroz, C. & Beale, G. H. (1974). Mitochondrial mutations affecting resistance to erythromycin and mikamycin in Paramecium aurelia: provisional results with a new method. Genetical Research 23, 233–238.CrossRefGoogle ScholarPubMed
Slonimski, P. P. & Tzagoloff, A. (1976). Localization in yeast mitochondrial DNA of mutations expressed in a deficiency of cytochrome oxidase and/or coenzyme QH2-cytochrome c reductase. European Journal of Biochemistry 61, 27–41.CrossRefGoogle ScholarPubMed