Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1773, Issue 3, Pages 321-329Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2006.10.009
Keywords
aldo-keto reductase; aldose reductase; Saccharomyces cerevisiae; mutagenesis; heat shock
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Funding
- NEI NIH HHS [P30 EY002687, R01 EY005856, EY05856, EY02687] Funding Source: Medline
- NIDDK NIH HHS [DK20579, P60 DK020579, P30 DK020579] Funding Source: Medline
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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. (c) 2006 Elsevier B.V. All rights reserved.
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