MET17and Hydrogen Sulfide Formation inSaccharomyces cerevisiae
- 1 October 2000
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 66 (10) , 4421-4426
- https://doi.org/10.1128/aem.66.10.4421-4426.2000
Abstract
Commercial isolates ofSaccharomyces cerevisiaediffer in the production of hydrogen sulfide (H2S) during fermentation, which has been attributed to variation in the ability to incorporate reduced sulfur into organic compounds. We transformed two commercial strains (UCD522 and UCD713) with a plasmid overexpressing theMET17gene, which encodes the bifunctionalO-acetylserine/O-acetylhomoserine sulfhydrylase (OAS/OAH SHLase), to test the hypothesis that the level of activity of this enzyme limits reduced sulfur incorporation, leading to H2S release. Overexpression ofMET17resulted in a 10- to 70-fold increase in OAS/OAH SHLase activity in UCD522 but had no impact on the level of H2S produced. In contrast, OAS/OAH SHLase activity was not as highly expressed in transformants of UCD713 (0.5- to 10-fold) but resulted in greatly reduced H2S formation. Overexpression of OAS/OAH SHLase activity was greater in UCD713 when grown under low-nitrogen conditions, but the impact on reduction of H2S was greater under high-nitrogen conditions. Thus, there was not a good correlation between the level of enzyme activity and H2S production. We measured cellular levels of cysteine to determine the impact of overexpression of OAS/OAH SHLase activity on sulfur incorporation. While Met17p activity was not correlated with increased cysteine production, conditions that led to elevated cytoplasmic levels of cysteine also reduced H2S formation. Our data do not support the simple hypothesis that variation in OAS/OAH SHLase activity is correlated with H2S production and release.Keywords
This publication has 41 references indexed in Scilit:
- High efficiency transformation of Escherichia coli with plasmidsPublished by Elsevier ,2003
- Determination of sulphite reductase activity and its response to assimilable nitrogen status in a commercial Saccharomyces cerevisiae wine yeastJournal of Applied Bacteriology, 1996
- Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilationJournal of General Microbiology, 1992
- The formation of dimethyl sulphide during fermentation using a wine yeastFood Microbiology, 1986
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- HYDROGEN SULFIDE EVOLUTION DUE TO PANTOTHENIC ACID DEFICIENCY IN THE YEAST REQUIRING THIS VITAMIN, WITH SPECIAL REFERENCE TO THE EFFECT OF ADENOSINE TRIPHOSPHATE ON YEAST CYSTEINE DESULFHYDRASEThe Journal of General and Applied Microbiology, 1973
- Production of H2S by Yeasts: Role of NutrientsJournal of Applied Bacteriology, 1971
- Hydrogen Sulphide Production by Yeast under Conditions of Methionine, Pantothenate or Vitamin B6 DeficiencyJournal of General Microbiology, 1970
- Nature, origin and prevention of hydrogen sulphide aroma in winesJournal of the Science of Food and Agriculture, 1963