H2O2 induces rapid biophysical and permeability changes in the plasma membrane of Saccharomyces cerevisiae

In Saccharomyces cerevisiae, the diffusion rate of hydrogen peroxide (H2O2) through the plasma membrane decreases during adaptation to H2O2 by means of a mechanism that is still unknown. Here, evidence is presented that during adaptation to H2O2 the anisotropy of the plasma membrane increases. Adapt...

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Published in:Biochimica et biophysica acta 2008-04, Vol.1778 (4), p.1141-1147
Main Authors: Folmer, Vanderlei, Pedroso, Nuno, Matias, Ana C, Lopes, Sílvia C D N, Antunes, Fernando, Cyrne, Luísa, Marinho, H Susana
Format: Article
Language:English
Subjects:
Adaptation, Physiological - drug effects
Anisotropy
Aquaporins - metabolism
Biological Transport - drug effects
Biophysical Phenomena
Biophysics
Cell Membrane Permeability - drug effects
Hydrogen Peroxide - pharmacology
Membrane Fluidity - drug effects
Mutation - genetics
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae Proteins - metabolism
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Summary:In Saccharomyces cerevisiae, the diffusion rate of hydrogen peroxide (H2O2) through the plasma membrane decreases during adaptation to H2O2 by means of a mechanism that is still unknown. Here, evidence is presented that during adaptation to H2O2 the anisotropy of the plasma membrane increases. Adaptation to H2O2 was studied at several times (15min up to 90min) by applying the steady-state H2O2 delivery model. For wild-type cells, the steady-state fluorescence anisotropy increased after 30min, or 60min, when using 2-(9-anthroyloxy) stearic acid (2-AS), or diphenylhexatriene (DPH) membrane probe, respectively. Moreover, a 40% decrease in plasma membrane permeability to H2O2 was observed at 15min with a concomitant two-fold increase in catalase activity. Disruption of the ergosterol pathway, by knocking out either ERG3 or ERG6, prevents the changes in anisotropy during H2O2 adaptation. H2O2 diffusion through the plasma membrane in S. cerevisiae cells is not mediated by aquaporins since the H2O2 permeability constant is not altered in the presence of the aquaporin inhibitor mercuric chloride. Altogether, these results indicate that the regulation of the plasma membrane permeability towards H2O2 is mediated by modulation of the biophysical properties of the plasma membrane.
ISSN:0006-3002
0005-2736
DOI:10.1016/j.bbamem.2007.12.008