Function of glycolytic bypass and S-lactoylglutathione in sporulation of yeast cells |
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| Institution: | 1. Department of Biomedical Sciences, Florida State University, Tallahassee, FL 32306, United States;2. Program in Neuroscience, Florida State University, Tallahassee, FL 32306, United States;3. Department of Psychology, Florida State University, Tallahassee, FL 32306, United States;1. Department of Pediatrics, The Queen Silvia Children''s Hospital, University of Gothenburg, Gothenburg, Sweden;2. Department of Pathology and Genetics, University of Gothenburg, Gothenburg, Sweden;3. Department of Clinical Chemistry, University of Gothenburg, Gothenburg, Sweden;4. Department of Pediatric Radiology, The Queen Silvia Children''s Hospital, University of Gothenburg, Gothenburg, Sweden;1. Department of Chemistry, University of Rochester, Rochester, New York;2. Department of Pediatrics and Neonatology, University of Rochester Medical Center, School of Medicine and Dentistry, University of Rochester, Rochester, New York |
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| Abstract: | When vegetative cells of a yeast Saccharomyces cerevisiae were incubated on sporulation medium, the cells were sporulated and thereby activities of methylglyoxal synthase and glyoxalase I, both of which are glycolytic bypass enzymes responsible for the conversion of dihydroxyacetone phosphate into S-lactoylglutathione, were preferentially and markedly increased. Sporulation was also enhanced in the presence of S-lactoylglutathione. We propose a possibility that the glycolytic bypass regulates the yeast cell sporulation and S-lactoylglutathione has a function to enhance the sporulation of yeast cells. |
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