Document Detail

Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress.
MedLine Citation:
PMID:  15060153     Owner:  NLM     Status:  MEDLINE    
Screening the Saccharomyces cerevisiae disruptome, profiling transcripts, and determining changes in protein expression have identified an important new role for the high-osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) pathway in the regulation of adaptation to citric acid stress. Deletion of HOG1, SSK1, PBS2, PTC2, PTP2, and PTP3 resulted in sensitivity to citric acid. Furthermore, citric acid resulted in the dual phosphorylation, and thus activation, of Hog1p. Despite minor activation of glycerol biosynthesis, the inhibitory effect of citric acid was not due to an osmotic shock. HOG1 negatively regulated the expression of a number of proteins in response to citric acid stress, including Bmh1p. Evidence suggests that BMH1 is induced by citric acid to counteract the effect of amino acid starvation. In addition, deletion of BMH2 rendered cells sensitive to citric acid. Deletion of the transcription factor MSN4, which is known to be regulated by Bmh1p and Hog1p, had a similar effect. HOG1 was also required for citric acid-induced up-regulation of Ssa1p and Eno2p. To counteract the cation chelating activity of citric acid, the plasma membrane Ca(2+) channel, CCH1, and a functional vacuolar membrane H(+)-ATPase were found to be essential for optimal adaptation. Also, the transcriptional regulator CYC8, which mediates glucose derepression, was required for adaptation to citric acid to allow cells to metabolize excess citrate via the tricarboxylic acid (TCA) cycle. Supporting this, Mdh1p and Idh1p, both TCA cycle enzymes, were up-regulated in response to citric acid.
Clare L Lawrence; Catherine H Botting; Robin Antrobus; Peter J Coote
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  24     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-04-02     Completed Date:  2004-05-19     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3307-23     Citation Subset:  IM    
Centre for Biomolecular Science, School of Biology, University of St. Andrews, St. Andrews, Fife KY16 9ST, United Kingdom.
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MeSH Terms
Adaptation, Biological / physiology*
Adenosine Triphosphatases / metabolism
Calcium Channels / metabolism
Citric Acid / metabolism*
Enzyme Activation
Gene Deletion
Gene Expression Profiling
Gene Expression Regulation, Fungal*
Genome, Fungal
MAP Kinase Signaling System / physiology*
Mitogen-Activated Protein Kinases / genetics,  metabolism*
Osmolar Concentration
Proteome / analysis
Saccharomyces cerevisiae / genetics,  growth & development,  metabolism*
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Reg. No./Substance:
0/Calcium Channels; 0/Proteome; 0/Saccharomyces cerevisiae Proteins; 56-81-5/Glycerol; 77-92-9/Citric Acid; EC 2.7.10.-/HOG1 protein, S cerevisiae; EC Protein Kinases; EC 3.6.1.-/Adenosine Triphosphatases

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