Cloning, sequence, and disruption of the Saccharom...[J Bacteriol. 1994]

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1: J Bacteriol. 1994 Nov;176(22):7091-5. Links

Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase.

Wang HT, Rahaim P, Robbins P, Yocum RR.

OmniGene, Inc., Cambridge, Massachusetts 02139-9002.

The Saccharomyces diastaticus DAR1 gene was cloned by complementation in an Escherichia coli strain auxogrophic for glycerol-3-phosphate. DAR1 encodes an NADH-dependent dihydroxyacetone phosphate reductase (sn-glycerol-3-phosphate dehydrogenase [G3PDase; EC 1.1.1.8]) homologous to several other eukaryotic G3PDases. DAR1 is distinct from GUT2, which encodes a glucose-repressed mitochondrial G3PDase, but is identical to GPD1 from S. cerevisiae, a close relative of S. diastaticus. The level of DAR1-encoded G3PDase was increased about threefold in a medium of high osmolarity. Disruption of DAR1 in a haploid S. cerevisiae was not lethal but led to a decrease in cytoplasmic NADH-dependent G3PDase activity, an increase in osmotic sensitivity, and a 25% reduction in glycerol secretion from cells grown anaerobically on glucose.

PMID: 7961476 [PubMed - indexed for MEDLINE]

PMCID: PMC197086

Cloning and characterization of GPD2, a second gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae, and its comparison with GPD1.
Mol Microbiol. 1995 Jul; 17(1):95-107.

[Mol Microbiol. 1995]
GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway.
Mol Cell Biol. 1994 Jun; 14(6):4135-44.

[Mol Cell Biol. 1994]
A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae.
Mol Microbiol. 1993 Dec; 10(5):1101-11.

[Mol Microbiol. 1993]
GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae.
Yeast. 1993 Oct; 9(10):1121-30.

[Yeast. 1993]
ReviewMolecular structure, developmental regulation, and evolution of the gene encoding glycerol-3-phosphate dehydrogenase isozymes in Drosophila melanogaster.
Prog Clin Biol Res. 1990; 344:341-74.

[Prog Clin Biol Res. 1990]
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Cited by 4 PubMed Central articles

The malate-aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast.
Easlon E, Tsang F, Skinner C, Wang C, Lin SJ. Genes Dev. 2008 Apr 1; 22(7):931-44.

[Genes Dev. 2008]
Expression of bacterial mtlD in Saccharomyces cerevisiae results in mannitol synthesis and protects a glycerol-defective mutant from high-salt and oxidative stress.
Chaturvedi V, Bartiss A, Wong B. J Bacteriol. 1997 Jan; 179(1):157-62.

[J Bacteriol. 1997]
Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae.
Björkqvist S, Ansell R, Adler L, Lidén G. Appl Environ Microbiol. 1997 Jan; 63(1):128-32.

[Appl Environ Microbiol. 1997]
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