Open AccessThiamine increases the resistance of baker's yeast Saccharomyces cerevisiae against oxidative, osmotic and thermal stress, through mechanisms partly independent of thiamine diphosphate‐bound enzymes
Author(s) -
Wolak Natalia,
Kowalska Ewa,
Kozik Andrzej,
RapalaKozik Maria
Publication year - 2014
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/1567-1364.12218
Subject(s) - thiamine , biochemistry , saccharomyces cerevisiae , yeast , biology , osmotic shock , oxidative stress , superoxide dismutase , enzyme , reactive oxygen species , gene
Numerous recent studies have established a hypothesis that thiamine (vitamin B 1 ) is involved in the responses of different organisms against stress, also suggesting that underlying mechanisms are not limited to the universal role of thiamine diphosphate ( TDP ) in the central cellular metabolism. The current work aimed at characterising the effect of exogenously added thiamine on the response of baker's yeast Saccharomyces cerevisiae to the oxidative (1 mM H 2 O 2 ), osmotic (1 M sorbitol) and thermal (42 °C) stress. As compared to the yeast culture in thiamine‐free medium, in the presence of 1.4 μM external thiamine, (1) the relative m RNA levels of major TDP‐dependent enzymes under stress conditions vs. unstressed control (the ‘stress/control ratio’) were moderately lower, (2) the stress/control ratio was strongly decreased for the transcript levels of several stress markers localised to the cytoplasm, peroxisomes, the cell wall and (with the strongest effect observed) the mitochondria (e.g. Mn‐superoxide dismutase), (3) the production of reactive oxygen and nitrogen species under stress conditions was markedly decreased, with the significant alleviation of concomitant protein oxidation. The results obtained suggest the involvement of thiamine in the maintenance of redox balance in yeast cells under oxidative stress conditions, partly independent of the functions of TDP‐dependent enzymes.