Open AccessPhysiological and genome‐wide transcriptional responses of Saccharomyces cerevisiae to high carbon dioxide concentrations
Author(s) -
Aguilera Jaime,
Petit Thomas,
Winde Johannes H.,
Pronk Jack T.
Publication year - 2005
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 - 10.1016/j.femsyr.2004.09.009
Subject(s) - chemostat , biology , carbonic anhydrase , bicarbonate , biochemistry , anaerobic exercise , phosphoenolpyruvate carboxylase , carbon dioxide , phosphoenolpyruvate carboxykinase , cellular respiration , respiratory chain , metabolism , saccharomyces cerevisiae , gene , mitochondrion , enzyme , bacteria , genetics , physiology , ecology , endocrinology
Physiological effects of carbon dioxide and impact on genome‐wide transcript profiles were analysed in chemostat cultures of Saccharomyces cerevisiae . In anaerobic, glucose‐limited chemostat cultures grown at atmospheric pressure, cultivation under CO 2 ‐saturated conditions had only a marginal (<10%) impact on the biomass yield. Conversely, a 25% decrease of the biomass yield was found in aerobic, glucose‐limited chemostat cultures aerated with a mixture of 79% CO 2 and 21% O 2 . This observation indicated that respiratory metabolism is more sensitive to CO 2 than fermentative metabolism. Consistent with the more pronounced physiological effects of CO 2 in respiratory cultures, the number of CO 2 ‐responsive transcripts was higher in aerobic cultures than in anaerobic cultures. Many genes involved in mitochondrial functions showed a transcriptional response to elevated CO 2 concentrations. This is consistent with an uncoupling effect of CO 2 and/or intracellular bicarbonate on the mitochondrial inner membrane. Other transcripts that showed a significant transcriptional response to elevated CO 2 included NCE103 (probably encoding carbonic anhydrase), PCK1 (encoding PEP carboxykinase) and members of the IMD gene family (encoding isozymes of inosine monophosphate dehydrogenase).