rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
1773
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
321-9
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pubmed:dateRevised |
2011-2-14
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pubmed:meshHeading |
pubmed-meshheading:17140678-Alcohol Oxidoreductases,
pubmed-meshheading:17140678-Gene Deletion,
pubmed-meshheading:17140678-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:17140678-Gene Expression Regulation, Fungal,
pubmed-meshheading:17140678-Hydrogen-Ion Concentration,
pubmed-meshheading:17140678-Kinetics,
pubmed-meshheading:17140678-Mutation,
pubmed-meshheading:17140678-Phenotype,
pubmed-meshheading:17140678-Saccharomyces cerevisiae
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pubmed:year |
2007
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pubmed:articleTitle |
Functional studies of aldo-keto reductases in Saccharomyces cerevisiae.
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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.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|