ArticleNucleic acids research2019
Activation of Haa1 and War1 transcription factors by differential binding of weak acid anions in Saccharomyces cerevisiae.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed.
- Sorbic acid triggers rapid formation of proteasome storage granules inMicrobial cell (Graz, Austria) · 2026Article
- Detection of Spoilage-Associated Acetic Acid Levels Using a Transcription-Based Whole-Cell Biosensor.Microbial biotechnology · 2025Article
- Calcium Signaling Is a Universal Carbon Source Signal Transducer and Effects an Ionic Memory of Past Carbon Sources.International journal of molecular sciences · 2025Article
- The transcription factor CgHaa1 plays a role in virulence of the pathogenic yeast Candida glabrata.FEMS yeast research · 2025Article
- Response mechanism of Saccharomyces cerevisiae under benzoic acid stress in ethanol fermentation.Scientific reports · 2024Article
- Protein Kinase A Negatively Regulates the Acetic Acid Stress Response inMicroorganisms · 2024Article
- Transcriptome analysis of Kluyveromyces marxianus under succinic acid stress and development of robust strains.Applied microbiology and biotechnology · 2024Article
- Just around the Corner: Advances in the Optimization of Yeasts and Filamentous Fungi for Lactic Acid Production.Journal of fungi (Basel, Switzerland) · 2024Review
- Mechanisms of antifungal resistance and developments in alternative strategies to combat Candida albicans infection.Archives of microbiology · 2024Review
- The role of ion homeostasis in adaptation and tolerance to acetic acid stress in yeasts.FEMS yeast research · 2024Review
- Development of an Haa1-Based Biosensor for Acetic Acid Sensing in Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2024Article
- General mechanisms of weak acid-tolerance and current strategies for the development of tolerant yeasts.World journal of microbiology & biotechnology · 2023Review
- Adaptive laboratory evolution under acetic acid stress enhances the multistress tolerance and ethanol production efficiency of Pichia kudriavzevii from lignocellulosic biomass.Scientific reports · 2023Article
- Regulation of acetate tolerance by small ORF-encoded polypeptides modulating efflux pump specificity in Methylomonas sp. DH-1.Biotechnology for biofuels and bioproducts · 2023Article
- Engineering Flocculation for Improved Tolerance and Production of d-Lactic Acid inJournal of fungi (Basel, Switzerland) · 2023Article
- The polyHIS Tract of Yeast AMPK Coordinates Carbon Metabolism with Iron Availability.International journal of molecular sciences · 2023Article
- Metabolic Engineering and Adaptive Evolution for Efficient Production of l-Lactic Acid in Saccharomyces cerevisiae.Microbiology spectrum · 2022Article
- Identification of acetic acid sensitive strains through biosensor-based screening of a Saccharomyces cerevisiae CRISPRi library.Microbial cell factories · 2022Article
- Combined roles of exporters in acetic acid tolerance in Saccharomyces cerevisiae.Biotechnology for biofuels and bioproducts · 2022Article
- Enhancing biofuels production by engineering the actin cytoskeleton in Saccharomyces cerevisiae.Nature communications · 2022Article
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5 authors.
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Abstract
In Saccharomyces cerevisiae, Haa1 and War1 transcription factors are involved in cellular adaptation against hydrophilic weak acids and lipophilic weak acids, respectively. However, it is unclear how these transcription factors are differentially activated depending on the identity of the weak acid. Using a field-effect transistor (FET)-type biosensor based on carbon nanofibers, in the present study we demonstrate that Haa1 and War1 directly bind to various weak acid anions with different affinities. Haa1 is most sensitive to acetate, followed by lactate, whereas War1 is most sensitive to benzoate, followed by sorbate, reflecting their differential activation during weak acid stresses. We show that DNA binding by Haa1 is induced in the presence of acetic acid and that the N-terminal Zn-binding domain is essential for this activity. Acetate binds to the N-terminal 150-residue region, and the transcriptional activation domain is located between amino acid residues 230 and 483. Our data suggest that acetate binding converts an inactive Haa1 to the active form, which is capable of DNA binding and transcriptional activation.
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