Hostname: page-component-745bb68f8f-f46jp Total loading time: 0 Render date: 2025-01-12T10:45:50.519Z Has data issue: false hasContentIssue false
  • English
  • Français

Inhibition of mitochondrial synthesis in yeast by erythromycin: cytoplasmic and nuclear factors controlling resistance

Published online by Cambridge University Press:  14 April 2009

D. Y. Thomas  and
D. Wilkie
D. Y. Thomas
Affiliation:
Botany Department, University College London
D. Wilkie
Affiliation:
Botany Department, University College London
Rights & Permissions [Opens in a new window]

Extract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Erythromycin-resistant mutants were separated into two categories showing Mendelian and non-Mendelian inheritance of resistance respectively. The cytoplasmic factor was located in the mitochondrion based on the fact that the loss of the mitochondrial genetic unit associated with the petite mutation (the ρ factor, assumed to be the mitochondrial DNA) resulted in a corresponding permanent loss of resistance. Conversely, the petite mutation in gene resistant mutants had no effect on the inheritance of resistance.

Analysis of vegetative and sexual progeny of isolated zygotes from a number of crosses between resistant and sensitive strains indicated that different mitochondrial types, both sensitive and resistant, co-exist in the yeast cell and are distributed at random among daughter cells under non-selective conditions. Only resistant mitochondria are in evidence if zygotes are put down to proliferate on medium containing the antibiotic.

Resistant strains were tested for retention of resistance following anaerobic culture (known to cause disruption of mitochondria). The cytoplasmic mutants retained their resistance but two gene-resistant mutants tested both lost their resistance. It was suggested in the latter case that resistance is dependent on the existence of intact mitochondrial membrane (possibly inner membrane). In the former mutants the mechanism of resistance may be the alteration of one or other of the components of the protein-synthesizing system of the organelle.

Type
Research Article
Information
Genetics Research , Volume 11 , Issue 1 , February 1968 , pp. 33 - 41
Copyright
Copyright © Cambridge University Press 1968

References

REFERENCES

Beavan, E. A. & Woods, R. A. (1964). In Teaching Genetics, ed. Darlington, C. D. and Bradshaw, A. D.. Edinburgh: Oliver and Boyd.Google Scholar
Clark-Walker, G. D. & Linnane, A. W. (1966). In vivo differentiation of yeast cytoplasmic and mitochondrial protein synthesis with antibiotics. Biochem. biophys. Res. Commun. 25, 8–13.CrossRefGoogle ScholarPubMed
Clark-Walker, G. D. & Linnane, A. W. (1967). Biogenesis of mitochondria in Saccharo-myces cerevisiae. J. Cell Biol. 34, 1–14.CrossRefGoogle Scholar
Cooper, D., Banthorpe, D. V. & Wilkie, D. (1967). Modified ribosomes conferring resistance to cycloheximide in mutants of Saccharomyces cerevisiae. J. molec. Biol. 26, 347–350.CrossRefGoogle ScholarPubMed
Corneo, G., Moore, C., Sanadi, D. R., Grossman, L. I. & Marmur, J. (1966). Mitochondrial DNA in yeast. Science, N.Y. 151, 687–690.Google Scholar
Ephrussi, B. (1953). Nucleo-cytoplasmic relationships in micro-organisms. Oxford: Clarendon Press.Google Scholar
Hawthorne, D. C. & Mortimer, R. K. (1960). Chromosome mapping in Saccharomyces. Genetics 45, 1085–1110.CrossRefGoogle ScholarPubMed
Linnane, A. W. (1967). In Biochemical Aspects of the Biogenesis of Mitochondria. Ed. Tager, Slater, Papa and Quagliariello, Adriatica Editrice, Bari. (In the Press.)Google Scholar
Lukins, H. B., Tham, S. H., Wallace, P. G. & Linnane, A. W. (1966). Correlation of membrane-bound succinate dehydrogenase with mitochondrial profiles in Saccharomyces cerevisiae. Biochem. biophys. Res. Commun. 23, 363–367.CrossRefGoogle ScholarPubMed
Mounolou, J., Jakob, H. & Slonimski, P. P. (1966). Mitochondrial DNA from yeast petite mutants: specific changes in buoyant density corresponding to different cytoplasmic mutations. Biochem. biophys. Res. Commun. 24, 218–224.CrossRefGoogle ScholarPubMed
Moustacchi, E. & Williams, D. H. (1966). Physiological variation in satellite components of yeast DNA detected by density gradient centrifugation. Biochem. biophys. Res. Commun. 23, 56–61.Google Scholar
Roodyn, D. B. & Wilkie, D. (1967 a). A characteristic pattern of respiratory enzymes in cytoplasmic petite strains of Saccharomyces cerevisiae as revealed by multiple enzyme analysis. Biochem. J. 103, 3c–5c.Google Scholar
Roodyn, D. B. & Wilkie, D. (1967 b). The Biogenesis of Mitochondria. London: Methuen. (In the Press.)Google Scholar
Sherman, F. & Slontmski, P. P. (1964). Respiratory deficient mutants of yeast. 11. Biochemistry. Biochim. biophys. Acta 90, 1–15.CrossRefGoogle Scholar
Sinclair, J. H., Stevens, B. J., Sanghavi, P. & Rabinowitz, M. (1967). Mitochondrial satellite and circular DNA filaments in yeast. Science, N.Y. 156, 1234–1237.CrossRefGoogle ScholarPubMed
Slonimski, P. P. (1953). In Formation des enzymes respiratoires chez la levure. Paris: Masson.Google Scholar
Tewari, K. K., Votch, W., Mahler, H. R. & Mackler, B. (1966). Biochemical correlates of respiratory deficiency. VI. Mitochondrial DNA. J. molec. Biol. 20, 453–481.Google Scholar
Vazquez, D. (1966). Binding of chloramphenicol to ribosomes: the effect of a number of antibiotics. Biochim. biophys. Acta 114, 277–288.Google Scholar
Wickerham, L. J. (1955). New materials and procedures for genetic studies of yeasts. Nature, Lond. 176, 22.Google Scholar
Wilkie, D. (1967). In Biochemical Aspects of the Biogenesis of Mitochondria. Ed. Tager, Slater, Papa and Quagliariello, Adriatica Editrice, Bari. (In the Press.)Google Scholar
Wilkie, D., Saunders, G. & Linnane, A. W. (1967). Inhibition of respiratory enzyme synthesis in yeast by chloramphenicol; relationship between chloramphenicol tolerance and resistance to other antibacterial antibiotics. Genet. Res., Camb. 10, 105–109.Google Scholar
Wintersberger, E. (1965). Proteinsynthese in isolierten Hefe-Mitochondrien. Biochem. Z. 341, 409–419.Google Scholar
Woodward, D. O. & Munkres, K. D. (1966). Alterations of a maternally inherited mitochondrial structural protein in respiratory deficient strains of Neurospora. Proc. natn. Acad. Sci., U.S.A. 55, 872–880.Google Scholar
Yotsuyanagi, Y. (1962). Etudes sur la chondriome de la levure. J. Ultrastruct. Res. 7, 121–129.CrossRefGoogle Scholar