Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-2-26
pubmed:abstractText
We utilized the budding yeast Saccharomyces cerevisiae as a model to systematically explore physiological roles for yeast and mammalian aldo-keto reductases. Six open reading frames encoding putative aldo-keto reductases were identified when the yeast genome was queried against the sequence for human aldose reductase, the prototypical mammalian aldo-keto reductase. Recombinant proteins produced from five of these yeast open reading frames demonstrated NADPH-dependent reductase activity with a variety of aldehyde and ketone substrates. A triple aldo-keto reductase null mutant strain demonstrated a glucose-dependent heat shock phenotype which could be rescued by ectopic expression of human aldose reductase. Catalytically-inactive mutants of human or yeast aldo-keto reductases failed to effect a rescue of the heat shock phenotype, suggesting that the phenotype results from either an accumulation of one or more unmetabolized aldo-keto reductase substrates or a synthetic deficiency of aldo-keto reductase products generated in response to heat shock stress. These results suggest that multiple aldo-keto reductases fulfill functionally redundant roles in the stress response in yeast.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-10407268, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-10818358, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-10913167, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-11032718, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-11460589, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-11481678, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-11884642, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-12198816, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-12210903, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-12271459, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-15094999, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-1516817, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-1520300, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-15564669, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-1562604, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-1611672, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-1621098, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-2105661, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-2123194, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-2901985, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-3014651, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-3025832, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-3130520, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-3280554, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7479844, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7510692, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7578036, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7586028, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7731983, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-7747971, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8117659, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8244985, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8245005, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8413288, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8554593, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8598053, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8628275, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8649403, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8718859, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8841374, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-8943244, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9038161, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9058981, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9094415, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9399804, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9483801, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9521675, http://linkedlifedata.com/resource/pubmed/commentcorrection/17140678-9920381
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1773
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-9
pubmed:dateRevised
2011-2-14
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Functional studies of aldo-keto reductases in Saccharomyces cerevisiae.
pubmed:affiliation
Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, 660 South Euclid Avenue (Campus Box 8096), St. Louis, MO 63110, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural