Current Genetics

, Volume 17, Issue 6, pp 465–472

Isolation and genetic study of Triethyltin-resistant mutants of Saccharomyces cerevisiae

  • C. H. Dupont
  • M. Rigoulet
  • M. Aigle
  • B. Guérin
Original Articles

DOI: 10.1007/BF00313073

Cite this article as:
Dupont, C.H., Rigoulet, M., Aigle, M. et al. Curr Genet (1990) 17: 465. doi:10.1007/BF00313073


Three mutants of Saccharomyces cerevisiae resistant to triethyltin (an inhibitor of mitochondrial ATPase) on non-fermentative media, and non-resistant to this drug on fermentative media, were isolated and named TTR1, TTR2 and TTR3. Apart from triethyltin resistance, these mutants show the following common characteristics: (1) Increased intracellular cytochrome c concentration. (2) Increased respiration rate. (3) Decreased growth yield. (4) Increased growth sensitivity to several drugs inhibiting oxidative phosphorylation: namely, CCCP (permeabilizing inner mitochondrial membrane to protons), valinomycin (permeabilizing inner mitochondrial membrane to potassium) and oligomycin (inhibitor of mitochondrial ATPase). (5) Increased sensitivity to carbon source starvation. For each mutant, these characteristics appeared to be due to a single pleiotropic nuclear mutation. Mutation TTR1 causes additional phenotypic characteristics which do not appear in mutants TTR2 and TTR3: (1) Pinkish coloration of colonies which is more pronounced after a long growth period. (2) Inability of the cells to store glycogen. (3) Growth defect of the cells on a galactose-containing medium. (4) Inability of a diploid homozygote mutant strain to sporulate. All these phenotypic characteristics have already been described in yeast mutants deregulated in cAMP-dependant protein phosphorylation. Crossing of a strain bearing the TTR1 mutation with a strain mutated in the adenylate cyclase structural gene suggested that the TTR1 phenotype is due to a modification in regulation of cAPK by cAMP, making cell multiplication possible without intracellular cAMP.

Key words

YeastMutantTriethyltin chlorideProtein phosphorylation



Cyclic Adenosine-3′-5′-monophosphate


cAMP-dependent protein kinase


carbonylcyanide m-chlorophenylhydrazone


Optical density


triethyltin chloride

Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • C. H. Dupont
    • 1
  • M. Rigoulet
    • 1
  • M. Aigle
    • 2
  • B. Guérin
    • 1
  1. 1.Institut de Biochimie Cellulaire et Neurochimie du CNRSBordeaux CedexFrance
  2. 2.Laboratoire de Génétique, allées des FacultésTalenceFrance