Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica
Abstract Background Yarrowia lipolytica is a dimorphic fungus, which switches from yeast to filament form in response to environmental conditions. For industrial purposes it is important to lock cells in the yeast or filamentous form depending on the fermentation process. yl-Hog1 kinase is a key com...
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| Format: | Article |
| Language: | English |
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BMC
2023-08-01
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| Series: | Microbial Cell Factories |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s12934-023-02161-8 |
| _version_ | 1797555526521847808 |
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| author | Dorota A. Rzechonek Mateusz Szczepańczyk Aleksandra M. Mirończuk |
| author_facet | Dorota A. Rzechonek Mateusz Szczepańczyk Aleksandra M. Mirończuk |
| author_sort | Dorota A. Rzechonek |
| collection | DOAJ |
| description | Abstract Background Yarrowia lipolytica is a dimorphic fungus, which switches from yeast to filament form in response to environmental conditions. For industrial purposes it is important to lock cells in the yeast or filamentous form depending on the fermentation process. yl-Hog1 kinase is a key component of the HOG signaling pathway, responsible for activating the osmotic stress response. Additionally, deletion of yl-Hog1 leads to increased filamentation in Yarrowia lipolytica, but causes significant sensitivity to osmotic stress induced by a high concentration of a carbon source. Results In this study, we tested the effect of point mutations on the function of yl-Hog1 protein kinase. The targets of modification were the phosphorylation sites (T171A-Y173A) and the active center (K49R). Introduction of the variant HOG1-49 into the hog1∆ strain partially improved growth under osmotic stress, but did not recover the yeast-like shape of the cells. The HOG1-171/173 variant was not functional, and its introduction further weakened the growth of hog1∆ strains in hyperosmotic conditions. To verify a genetic modification in filament form, we developed a new system based on green fluorescent protein (GFP) for easier screening of proper mutants. Conclusions These results provide new insights into the functions of yl-Hog1 protein in dimorphic transition and constitute a good starting point for further genetic modification of Y. lipolytica in filament form. |
| first_indexed | 2024-03-10T16:48:46Z |
| format | Article |
| id | doaj.art-68399a292f744d9ab4a669ca4f474159 |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-03-10T16:48:46Z |
| publishDate | 2023-08-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-68399a292f744d9ab4a669ca4f4741592023-11-20T11:22:21ZengBMCMicrobial Cell Factories1475-28592023-08-0122111310.1186/s12934-023-02161-8Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolyticaDorota A. Rzechonek0Mateusz Szczepańczyk1Aleksandra M. Mirończuk2Laboratory for Biosustainability, Institute of Environmental Biology, Wrocław University of Environmental and Life SciencesLaboratory for Biosustainability, Institute of Environmental Biology, Wrocław University of Environmental and Life SciencesLaboratory for Biosustainability, Institute of Environmental Biology, Wrocław University of Environmental and Life SciencesAbstract Background Yarrowia lipolytica is a dimorphic fungus, which switches from yeast to filament form in response to environmental conditions. For industrial purposes it is important to lock cells in the yeast or filamentous form depending on the fermentation process. yl-Hog1 kinase is a key component of the HOG signaling pathway, responsible for activating the osmotic stress response. Additionally, deletion of yl-Hog1 leads to increased filamentation in Yarrowia lipolytica, but causes significant sensitivity to osmotic stress induced by a high concentration of a carbon source. Results In this study, we tested the effect of point mutations on the function of yl-Hog1 protein kinase. The targets of modification were the phosphorylation sites (T171A-Y173A) and the active center (K49R). Introduction of the variant HOG1-49 into the hog1∆ strain partially improved growth under osmotic stress, but did not recover the yeast-like shape of the cells. The HOG1-171/173 variant was not functional, and its introduction further weakened the growth of hog1∆ strains in hyperosmotic conditions. To verify a genetic modification in filament form, we developed a new system based on green fluorescent protein (GFP) for easier screening of proper mutants. Conclusions These results provide new insights into the functions of yl-Hog1 protein in dimorphic transition and constitute a good starting point for further genetic modification of Y. lipolytica in filament form.https://doi.org/10.1186/s12934-023-02161-8Yarrowia lipolyticaOsmotic stressErythritolDimorphic transition |
| spellingShingle | Dorota A. Rzechonek Mateusz Szczepańczyk Aleksandra M. Mirończuk Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica Microbial Cell Factories Yarrowia lipolytica Osmotic stress Erythritol Dimorphic transition |
| title | Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica |
| title_full | Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica |
| title_fullStr | Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica |
| title_full_unstemmed | Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica |
| title_short | Mutation in yl-HOG1 represses the filament-to-yeast transition in the dimorphic yeast Yarrowia lipolytica |
| title_sort | mutation in yl hog1 represses the filament to yeast transition in the dimorphic yeast yarrowia lipolytica |
| topic | Yarrowia lipolytica Osmotic stress Erythritol Dimorphic transition |
| url | https://doi.org/10.1186/s12934-023-02161-8 |
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