Author:

Keywords:

kluyveromyces lactis, adh, allyl alcohol, nadph, pentose-phosphate pathway, saccharomyces-cerevisiae, redox balance, yeast, glucose, mutants, fermentation, induction, multiple, Science & Technology, Life Sciences & Biomedicine, Biotechnology & Applied Microbiology, Microbiology, Mycology, Kluyveromyces lactis, ADH, NADPH, PENTOSE-PHOSPHATE PATHWAY, SACCHAROMYCES-CEREVISIAE, REDOX BALANCE, YEAST, GLUCOSE, MUTANTS, FERMENTATION, INDUCTION, MULTIPLE, Alcohol Dehydrogenase, Cytochromes, Cytosol, Electron Transport, Electron Transport Chain Complex Proteins, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Kluyveromyces, Mitochondria, Mitochondrial Proteins, Mutation, NADP, 06 Biological Sciences, 09 Engineering, 10 Technology, 31 Biological sciences, 40 Engineering

Abstract:

A Kluyveromyces lactis strain, harbouring KlADH3 as the unique alcohol dehydrogenase (ADH) gene, was used in a genetic screen on allyl alcohol to isolate mutants deregulated in the expression of this gene. Here we report the characterization of some mutants that lacked or had highly reduced amounts of KlAdh3p activity; in addition, these mutants showed alterations in glucose metabolism, reduced respiration and reduced cytochrome content. Our results confirm that the KlAdh3p activity contributes to the reoxidation of cytosolic NAD(P)H feeding the respiratory chain through KlNdi1p, the mitochondrial internal transdehydrogenase. The low levels of KlAdh3p in two of the mutants were associated with mutations in KlSDH1, one of the genes of complex II, suggesting signalling between the respiratory chain and expression of the KlADH3 gene.