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Research was conducted to examine the hypothesis that the lactate-proton symport of Saccharomyces cerevisiae is encoded by the gene JEN10. The isolation of the mutant of S. cerevisiae that was deficient in lactate-proton was performed by transforming the mutant with a yeast genomic library. Results suggest that no other monocarboxylate permease can efficiently transport lactate in S. cerevisiae under the experimental conditions examined.

Unspecific bacterial reduction of azo dyes is a process widely studied in correlation with the biological treatment of colored wastewaters, but the enzyme system associated with this bacterial capability has never been positively identified. Several ascomycete yeast strains display similar decolorizing behaviors. The yeast-mediated process requires an alternative carbon and energy source and is independent of previous exposure to the dyes. When substrate dyes are polar, their reduction is extracellular, strongly suggesting the involvement of an externally directed plasma membrane redox system. The present work demonstrates that, in Saccharomyces cerevisiae, the ferric reductase system participates in the extracellular reduction of azo dyes. The S. cerevisiae Δfre1 and Δfre1 Δfre2 mutant strains, but not the Δfre2 strain, showed much reduced decolorizing capabilities. The ΔRE1 gene complemented the phenotype of S. cerevisiae Δfre1 cells, restoring the ability to grow in medium without externally added iron and to decolorize the dye, following a pattern similar to the one observed in the wild-type strain. These results suggest that under the conditions tested, Fre1p is a major component of the azo reductase activity. [ABSTRACT FROM AUTHOR]