Abstract
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.
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Selected References
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- Albertyn J., Hohmann S., Thevelein J. M., Prior B. A. 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):4135–4144. doi: 10.1128/mcb.14.6.4135. [DOI] [PMC free article] [PubMed] [Google Scholar]
- André L., Hemming A., Adler L. Osmoregulation in Saccharomyces cerevisiae. Studies on the osmotic induction of glycerol production and glycerol-3-phosphate dehydrogenase (NAD+) FEBS Lett. 1991 Jul 29;286(1-2):13–17. doi: 10.1016/0014-5793(91)80930-2. [DOI] [PubMed] [Google Scholar]
- Austin D., Larson T. J. Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12. J Bacteriol. 1991 Jan;173(1):101–107. doi: 10.1128/jb.173.1.101-107.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Balakrishnan R., Frohlich M., Rahaim P. T., Backman K., Yocum R. R. Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca. J Biol Chem. 1993 Nov 25;268(33):24792–24795. [PubMed] [Google Scholar]
- Bewley G. C., Cook J. L., Kusakabe S., Mukai T., Rigby D. L., Chambers G. K. Sequence, structure and evolution of the gene coding for sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster. Nucleic Acids Res. 1989 Nov 11;17(21):8553–8567. doi: 10.1093/nar/17.21.8553. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Blomberg A., Adler L. Roles of glycerol and glycerol-3-phosphate dehydrogenase (NAD+) in acquired osmotolerance of Saccharomyces cerevisiae. J Bacteriol. 1989 Feb;171(2):1087–1092. doi: 10.1128/jb.171.2.1087-1092.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brewster J. L., de Valoir T., Dwyer N. D., Winter E., Gustin M. C. An osmosensing signal transduction pathway in yeast. Science. 1993 Mar 19;259(5102):1760–1763. doi: 10.1126/science.7681220. [DOI] [PubMed] [Google Scholar]
- Chen S. M., Trumbore M. W., Osinchak J. E., Merkel J. R. Improved purification and some molecular and kinetic properties of sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae. Prep Biochem. 1987;17(4):435–446. doi: 10.1080/00327488708062506. [DOI] [PubMed] [Google Scholar]
- Cole S. T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W. F., Weiner J. H. Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12. J Bacteriol. 1988 Jun;170(6):2448–2456. doi: 10.1128/jb.170.6.2448-2456.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cronan J. E., Jr, Bell R. M. Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of the structural gene for L-glycerol 3-phosphate dehydrogenase. J Bacteriol. 1974 May;118(2):598–605. doi: 10.1128/jb.118.2.598-605.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gancedo C., Gancedo J. M., Sols A. Glycerol metabolism in yeasts. Pathways of utilization and production. Eur J Biochem. 1968 Jul;5(2):165–172. doi: 10.1111/j.1432-1033.1968.tb00353.x. [DOI] [PubMed] [Google Scholar]
- Gancedo C., Llobell A., Ribas J. C., Luchi F. Isolation and characterization of mutants from Schyzosaccharomyces pombe defective in glycerol catabolism. Eur J Biochem. 1986 Aug 15;159(1):171–174. doi: 10.1111/j.1432-1033.1986.tb09848.x. [DOI] [PubMed] [Google Scholar]
- Hartl F. U., Pfanner N., Nicholson D. W., Neupert W. Mitochondrial protein import. Biochim Biophys Acta. 1989 Jan 18;988(1):1–45. doi: 10.1016/0304-4157(89)90002-6. [DOI] [PubMed] [Google Scholar]
- Ireland R. C., Kotarski M. A., Johnston L. A., Stadler U., Birkenmeier E., Kozak L. P. Primary structure of the mouse glycerol-3-phosphate dehydrogenase gene. J Biol Chem. 1986 Sep 5;261(25):11779–11785. [PubMed] [Google Scholar]
- Jollow D., Kellerman G. M., Linnane A. W. The biogenesis of mitochondria. 3. The lipid composition of aerobically and anaerobically grown Saccharomyces cerevisiae as related to the membrane systems of the cells. J Cell Biol. 1968 May;37(2):221–230. doi: 10.1083/jcb.37.2.221. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Larsson K., Ansell R., Eriksson P., Adler L. A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae. Mol Microbiol. 1993 Dec;10(5):1101–1111. doi: 10.1111/j.1365-2958.1993.tb00980.x. [DOI] [PubMed] [Google Scholar]
- Maeda T., Wurgler-Murphy S. M., Saito H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature. 1994 May 19;369(6477):242–245. doi: 10.1038/369242a0. [DOI] [PubMed] [Google Scholar]
- Merkel J. R., Straume M., Sajer S. A., Hopfer R. L. Purification and some properties of sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae. Anal Biochem. 1982 May 1;122(1):180–185. doi: 10.1016/0003-2697(82)90268-8. [DOI] [PubMed] [Google Scholar]
- Nader W., Betz A., Becker J. U. Partial purification, substrate specificity and regulation of alpha-L-glycerolphosphate dehydrogenase from Saccharomyces carlsbergensis. Biochim Biophys Acta. 1979 Dec 7;571(2):177–185. doi: 10.1016/0005-2744(79)90088-3. [DOI] [PubMed] [Google Scholar]
- Nasmyth K. A., Reed S. I. Isolation of genes by complementation in yeast: molecular cloning of a cell-cycle gene. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2119–2123. doi: 10.1073/pnas.77.4.2119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nordström K. Yeast growth and glycerol formation. Acta Chem Scand. 1966;20(4):1016–1025. doi: 10.3891/acta.chem.scand.20-1016. [DOI] [PubMed] [Google Scholar]
- Pidoux A. L., Fawell E. H., Armstrong J. Glycerol-3-phosphate dehydrogenase homologue from Schizosaccharomyces pombe. Nucleic Acids Res. 1990 Dec 11;18(23):7145–7145. doi: 10.1093/nar/18.23.7145. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rønnow B., Kielland-Brandt M. C. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Yeast. 1993 Oct;9(10):1121–1130. doi: 10.1002/yea.320091013. [DOI] [PubMed] [Google Scholar]
- Sengstag C. The sequence of Saccharomyces cerevisiae cloning vector pCS19 allowing direct selection for DNA inserts. Gene. 1993 Feb 14;124(1):141–142. doi: 10.1016/0378-1119(93)90778-2. [DOI] [PubMed] [Google Scholar]
- Sleep D., Ogden J. E., Roberts N. A., Goodey A. R. Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter. Gene. 1991 May 15;101(1):89–96. doi: 10.1016/0378-1119(91)90228-4. [DOI] [PubMed] [Google Scholar]
- Sprague G. F., Cronan J. E. Isolation and characterization of Saccharomyces cerevisiae mutants defective in glycerol catabolism. J Bacteriol. 1977 Mar;129(3):1335–1342. doi: 10.1128/jb.129.3.1335-1342.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yarrow D., Nakase T. DNA base composition of species of the genus Saccharomyces. Antonie Van Leeuwenhoek. 1975;41(1):81–88. doi: 10.1007/BF02565038. [DOI] [PubMed] [Google Scholar]
- de Vries S., Marres C. A. The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim Biophys Acta. 1987;895(3):205–239. doi: 10.1016/s0304-4173(87)80003-4. [DOI] [PubMed] [Google Scholar]
