The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i>
<i>Hanseniaspora uvarum</i> is the predominant yeast species in the majority of wine fermentations, which has only recently become amenable to directed genetic manipulation. The genetics and metabolism of <i>H. uvarum</i> have been poorly studied as compared to other yeasts o...
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MDPI AG
2024-02-01
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| Series: | International Journal of Molecular Sciences |
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| author | Jürgen J. Heinisch Andrea Murra Lucía Fernández Murillo Hans-Peter Schmitz |
| author_facet | Jürgen J. Heinisch Andrea Murra Lucía Fernández Murillo Hans-Peter Schmitz |
| author_sort | Jürgen J. Heinisch |
| collection | DOAJ |
| description | <i>Hanseniaspora uvarum</i> is the predominant yeast species in the majority of wine fermentations, which has only recently become amenable to directed genetic manipulation. The genetics and metabolism of <i>H. uvarum</i> have been poorly studied as compared to other yeasts of biotechnological importance. This work describes the construction and characterization of homozygous deletion mutants in the <i>HuZWF1</i> gene, encoding glucose-6-phosphate dehydrogenase (G6PDH), which provides the entrance into the oxidative part of the pentose phosphate pathway (PPP) and serves as a major source of NADPH for anabolic reactions and oxidative stress response. <i>Huzwf1</i> deletion mutants grow more slowly on glucose medium than wild-type and are hypersensitive both to hydrogen peroxide and potassium bisulfite, indicating that G6PDH activity is required to cope with these stresses. The mutant also requires methionine for growth. Enzyme activity can be restored by the expression of heterologous G6PDH genes from other yeasts and humans under the control of a strong endogenous promoter. These findings provide the basis for a better adaptation of <i>H. uvarum</i> to conditions used in wine fermentations, as well as its use for other biotechnological purposes and as an expression organism for studying G6PDH functions in patients with hemolytic anemia. |
| first_indexed | 2024-03-07T22:28:31Z |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-07T22:28:31Z |
| publishDate | 2024-02-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-4efe67c8d8e14d778c4ed408e6d39ccf2024-02-23T15:20:52ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-02-01254239510.3390/ijms25042395The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i>Jürgen J. Heinisch0Andrea Murra1Lucía Fernández Murillo2Hans-Peter Schmitz3AG Genetik, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastr. 11, D-49076 Osnabrück, GermanyAG Genetik, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastr. 11, D-49076 Osnabrück, GermanyAG Genetik, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastr. 11, D-49076 Osnabrück, GermanyAG Genetik, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastr. 11, D-49076 Osnabrück, Germany<i>Hanseniaspora uvarum</i> is the predominant yeast species in the majority of wine fermentations, which has only recently become amenable to directed genetic manipulation. The genetics and metabolism of <i>H. uvarum</i> have been poorly studied as compared to other yeasts of biotechnological importance. This work describes the construction and characterization of homozygous deletion mutants in the <i>HuZWF1</i> gene, encoding glucose-6-phosphate dehydrogenase (G6PDH), which provides the entrance into the oxidative part of the pentose phosphate pathway (PPP) and serves as a major source of NADPH for anabolic reactions and oxidative stress response. <i>Huzwf1</i> deletion mutants grow more slowly on glucose medium than wild-type and are hypersensitive both to hydrogen peroxide and potassium bisulfite, indicating that G6PDH activity is required to cope with these stresses. The mutant also requires methionine for growth. Enzyme activity can be restored by the expression of heterologous G6PDH genes from other yeasts and humans under the control of a strong endogenous promoter. These findings provide the basis for a better adaptation of <i>H. uvarum</i> to conditions used in wine fermentations, as well as its use for other biotechnological purposes and as an expression organism for studying G6PDH functions in patients with hemolytic anemia.https://www.mdpi.com/1422-0067/25/4/2395<i>ZWF1</i>pentose phosphate pathwaysulfite resistanceoxidative stresshuman G6PDH |
| spellingShingle | Jürgen J. Heinisch Andrea Murra Lucía Fernández Murillo Hans-Peter Schmitz The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> International Journal of Molecular Sciences <i>ZWF1</i> pentose phosphate pathway sulfite resistance oxidative stress human G6PDH |
| title | The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> |
| title_full | The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> |
| title_fullStr | The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> |
| title_full_unstemmed | The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> |
| title_short | The Role of Glucose-6-phosphate Dehydrogenase in the Wine Yeast <i>Hanseniaspora uvarum</i> |
| title_sort | role of glucose 6 phosphate dehydrogenase in the wine yeast i hanseniaspora uvarum i |
| topic | <i>ZWF1</i> pentose phosphate pathway sulfite resistance oxidative stress human G6PDH |
| url | https://www.mdpi.com/1422-0067/25/4/2395 |
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