Sulfur sparing in the yeast proteome in response to sulfur demand. Export

@article{fauchon2002, abstract = {Genome-wide studies have recently revealed the unexpected complexity of the genetic response to apparently simple physiological changes. Here, we show that when yeast cells are exposed to Cd(2+), most of the sulfur assimilated by the cells is converted into glutathione, a thiol-metabolite essential for detoxification. Cells adapt to this vital metabolite requirement by modifying globally their proteome to reduce the production of abundant sulfur-rich proteins. In particular, some abundant glycolytic enzymes are replaced by sulfur-depleted isozymes. This global change in protein expression allows an overall sulfur amino acid saving of 30\%. This proteomic adaptation is essentially regulated at the mRNA level. The main transcriptional activator of the sulfate assimilation pathway, Met4p, plays an essential role in this sulfur-sparing response.}, author = {Fauchon, M. and Lagniel, G. and Aude, J. C. and Lombardia, L. and Soularue, P. and Petat, C. and Marguerie, G. and Sentenac, A. and Werner, M. and Labarre, J.}, citeulike-article-id = {3424584}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11983164}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11983164}, comment = {Examines changes in yeast gene expression in response to sulfur limitation, resulting from exposure to cadmium. Cadmium induces a sulfur drain in the cell, where sulfur is required to sequester the cadmium. Authors found that gene expression changes to reduce amount of sulfur containing residues encoded in the proteome. The study also found that sulfur rich enzymes are also correspondingly replaces with sulfur depleted isoenzymes for the same function. The results suggests that these isoezymes are switched around depending on whether there is sulfur limitation or not.}, issn = {1097-2765}, journal = {Molecular cell}, keywords = {amino-acid-usage, cost-minimisation, gene-duplication, gene-expression, isoenzymes, mdb-thesis, nutrient-limitation, reviewed, sulfur}, month = {April}, number = {4}, pages = {713--723}, posted-at = {2008-10-17 15:17:09}, priority = {0}, title = {Sulfur sparing in the yeast proteome in response to sulfur demand.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11983164}, volume = {9}, year = {2002} }

TY - JOUR ID - fauchon2002 L3 - citeulike-article-id:3424584 N2 - Genome-wide studies have recently revealed the unexpected complexity of the genetic response to apparently simple physiological changes. Here, we show that when yeast cells are exposed to Cd(2+), most of the sulfur assimilated by the cells is converted into glutathione, a thiol-metabolite essential for detoxification. Cells adapt to this vital metabolite requirement by modifying globally their proteome to reduce the production of abundant sulfur-rich proteins. In particular, some abundant glycolytic enzymes are replaced by sulfur-depleted isozymes. This global change in protein expression allows an overall sulfur amino acid saving of 30%. This proteomic adaptation is essentially regulated at the mRNA level. The main transcriptional activator of the sulfate assimilation pathway, Met4p, plays an essential role in this sulfur-sparing response. IS - 4 JF - Molecular cell SN - 1097-2765 EP - 723 TI - Sulfur sparing in the yeast proteome in response to sulfur demand. VL - 9 SP - 713 KW - amino-acid-usage KW - cost-minimisation KW - gene-duplication KW - gene-expression KW - isoenzymes KW - mdb-thesis KW - nutrient-limitation KW - reviewed KW - sulfur N1 - Examines changes in yeast gene expression in response to sulfur limitation, resulting from exposure to cadmium. Cadmium induces a sulfur drain in the cell, where sulfur is required to sequester the cadmium. Authors found that gene expression changes to reduce amount of sulfur containing residues encoded in the proteome. The study also found that sulfur rich enzymes are also correspondingly replaces with sulfur depleted isoenzymes for the same function. The results suggests that these isoezymes are switched around depending on whether there is sulfur limitation or not. AU - Fauchon, M AU - Lagniel, G AU - Aude, JC AU - Lombardia, L AU - Soularue, P AU - Petat, C AU - Marguerie, G AU - Sentenac, A AU - Werner, M AU - Labarre, J PY - 2002/04// UR - http://view.ncbi.nlm.nih.gov/pubmed/11983164 ER -